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Do multiheme cytochromes containing close-packed heme groups have a band structure formed from the heme π and π* orbitals?
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Rhizobium etli is able to emit nitrous oxide by connecting assimilatory nitrate reduction with nitrite respiration in the bacteroids of common bean nodules.
Journal of Plant Interactions, 18 (1).
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Scientific Reports, 11.
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Microbial small RNAs – The missing link in the nitrogen cycle?
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Exploring the molecular machinery of denitrification in Haloferax mediterranei through proteomics.
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A dual functional redox enzyme maturation protein for respiratory and assimilatory nitrate reductases in bacteria.
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The Paracoccus denitrificans NarK-like nitrate and nitrite transporters; probing nitrate uptake and nitrate/nitrite exchange mechanisms.
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Genome-wide discovery of putative sRNAs in Paracoccus denitrificans expressed under nitrous oxide emitting conditions.
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Unexpected weak magnetic exchange coupling between haem and non-haem iron in the catalytic site of nitric oxide reductase (NorBC) from Paracoccus denitrificans.
Biochemical Journal, 451 (3).
pp. 389-394.
ISSN 0264-6021
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226 and Clarke, Thomas A.
ORCID: https://orcid.org/0000-0002-6234-1914
(2013)
Controlling electron transfer at the microbe-mineral interface.
Proceedings of the National Academy of Sciences of the United States of America (PNAS), 110 (19).
pp. 7537-7538.
ISSN 1091-6490
White, Gaye, Shi, Zhi, Shi, Liang, Wang, Zheming, Dohnalkova, Alice C., Marshall, Matthew J., Fredrickson, James K., Zachara, John M., Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Clarke, Thomas A.
ORCID: https://orcid.org/0000-0002-6234-1914
(2013)
Rapid electron exchange between surface-exposed bacterial cytochromes and Fe(III) minerals.
Proceedings of the National Academy of Sciences of the United States of America (PNAS), 110 (16).
pp. 6346-6351.
ISSN 1091-6490
Edwards, Marcus J., Fredrickson, James K., Zachara, John M., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Clarke, Thomas A.
ORCID: https://orcid.org/0000-0002-6234-1914
(2012)
Analysis of structural MtrC models based on homology with crystal structure of MtrF.
Biochemical Society Transactions, 40 (6).
pp. 1181-1185.
ISSN 0300-5127
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Fredrickson, James K. and Zachara, John M.
(2012)
Electron transport at the microbe-mineral interface: A synthesis of current research challenges.
Biochemical Society Transactions, 40 (6).
pp. 1163-1166.
ISSN 0300-5127
Edwards, Marcus J., Hall, Andrea, Shi, Liang, Fredrickson, James K., Zachara, John M., Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Clarke, Thomas A.
ORCID: https://orcid.org/0000-0002-6234-1914
(2012)
The crystal structure of the extracellular 11-heme cytochrome UndA reveals a conserved 10-heme motif and defined binding site for soluble iron chelates.
Structure, 20 (7).
pp. 1275-1284.
ISSN 1878-4186
Bueno, Emilio, Mesa, Socorro, Bedmar, Eulogio J., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Delgado, Maria J.
(2012)
Bacterial adaptation of respiration from oxic to microoxic and anoxic conditions:Redox control.
Antioxidants and Redox Signaling, 16 (8).
pp. 819-852.
ISSN 1523-0864
Shi, Liang, Rosso, Kevin M., Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832, Zachara, John M. and Fredrickson, James K.
(2012)
Molecular underpinnings of Fe(III) oxide reduction by Shewanella Oneidensis MR-1.
Frontiers in Microbiology, 3.
ISSN 1664-302X
Liu, Juan, Wang, Zheming, Belchik, Sara M., Edwards, Marcus J., Liu, Chongxuan, Kennedy, David W., Merkley, Eric D., Lipton, Mary S., Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832, Zachara, John M., Fredrickson, James K., Rosso, Kevin M. and Shi, Liang
(2012)
Identification and characterization of MtoA: A decaheme c-type cytochrome of the neutrophilic Fe(II)-oxidizing bacterium Sideroxydans lithotrophicus ES-1.
Frontiers in Microbiology, 3.
ISSN 1664-302X
Stremińska, Marta A., Felgate, Heather, Rowley, Gary ORCID: https://orcid.org/0000-0002-5421-4333, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Baggs, Elizabeth M.
(2012)
Nitrous oxide production in soil isolates of nitrate-ammonifying bacteria.
Environmental Microbiology Reports, 4 (1).
pp. 66-71.
ISSN 1758-2229
Rowley, Gary ORCID: https://orcid.org/0000-0002-5421-4333, Hensen, Daniela, Felgate, Heather, Arkenberg, Anke, Appia‑Ayme, Corinne, Prior, Karen, Harrington, Carl, Field, Sarah J., Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226, Baggs, Elizabeth and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2012)
Resolving the contributions of the membrane-bound and periplasmic nitrate reductase systems to nitric oxide and nitrous oxide production in Salmonella enterica serovar Typhimurium.
Biochemical Journal, 441 (2).
pp. 755-762.
ISSN 0264-6021
Breuer, Marian, Zarzycki, Piotr, Shi, Liang, Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Edwards, Marcus J., Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832, Fredrickson, James K., Zachara, John M., Blumberger, Jochen and Rosso, Kevin M.
(2012)
Molecular structure and free energy landscape for electron transport in the decahaem cytochrome MtrF.
Biochemical Society Transactions, 40 (6).
pp. 1198-1203.
ISSN 0300-5127
Felgate, Heather, Giannopoulos, George, Sullivan, Matthew J. ORCID: https://orcid.org/0000-0003-2276-3132, Gates, Andrew J.
ORCID: https://orcid.org/0000-0002-4594-5038, Clarke, Thomas A.
ORCID: https://orcid.org/0000-0002-6234-1914, Baggs, Elizabeth, Rowley, Gary
ORCID: https://orcid.org/0000-0002-5421-4333 and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2012)
The impact of copper, nitrate and carbon status on the emission of nitrous oxide by two species of bacteria with biochemically distinct denitrification pathways.
Environmental Microbiology, 14 (7).
pp. 1788-1800.
ISSN 1462-2920
Marritt, Sophie J., Lowe, Thomas G., Bye, Jordan, McMillan, Duncan G. G., Shi, Liang, Fredrickson, Jim, Zachara, John, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Cheesman, Myles R., Jeuken, Lars J. C. and Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226
(2012)
A functional description of CymA, an electron-transfer hub supporting anaerobic respiratory flexibility in Shewanella.
Biochemical Journal, 444 (3).
pp. 465-474.
ISSN 0264-6021
Marritt, Sophie J., McMillan, Duncan G.G., Shi, Liang, Fredrickson, James K., Zachara, John M., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Jeuken, LJC and Butt, JN
ORCID: https://orcid.org/0000-0002-9624-5226
(2012)
The roles of CymA in support of the respiratory flexibility of Shewanella oneidensis MR-1.
Biochemical Society Transactions, 40 (6).
pp. 1217-1221.
ISSN 0300-5127
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226, Fredrickson, Jim K., Zachara, John M., Shi, Liang, Edwards, Marcus J., White, Gaye, Baiden, Nanakow, Gates, Andrew J.
ORCID: https://orcid.org/0000-0002-4594-5038, Marritt, Sophie J. and Clarke, Thomas A.
ORCID: https://orcid.org/0000-0002-6234-1914
(2012)
The ‘porin-cytochrome’ model for microbe-to-mineral electron transfer.
Molecular Microbiology, 85 (2).
pp. 201-212.
ISSN 1365-2958
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Edwards, Marcus J., White, Gaye F., Baiden, Nanakow, Hartshorne, Robert S., Fredrickson, Jim, Shi, Liang, Zachara, John, Gates, Andrew J.
ORCID: https://orcid.org/0000-0002-4594-5038, Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226 and Clarke, Thomas A.
ORCID: https://orcid.org/0000-0002-6234-1914
(2012)
Exploring the biochemistry at the extracellular redox frontier of bacterial mineral Fe(III) respiration.
Biochemical Society Transactions, 40 (3).
pp. 493-500.
ISSN 0300-5127
White, Gaye F., Shi, Zhi, Shi, Liang, Dohnalkova, Alice C., Fredrickson, James K., Zachara, John M., Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Clarke, Thomas A.
ORCID: https://orcid.org/0000-0002-6234-1914
(2012)
Development of a proteoliposome model to probe transmembrane electron-transfer reactions.
Biochemical Society Transactions, 40 (6).
pp. 1257-1260.
ISSN 0300-5127
Arkenberg, Anke, Runkel, Sebastian, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Rowley, Gary
ORCID: https://orcid.org/0000-0002-5421-4333
(2011)
The production and detoxification of a potent cytotoxin, nitric oxide, by pathogenic enteric bacteria.
Biochemical Society Transactions, 39 (6).
pp. 1876-1879.
ISSN 0300-5127
Goddard, Alan D., Stevens, Julie M., Rao, Feng, Mavridou, Despoina A.I., Chan, Weelee, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Allen, James W.A. and Ferguson, Stuart J.
(2011)
c-Type cytochrome biogenesis can occur via a natural Ccm system lacking CcmH, CcmG, and the heme-binding histidine of CcmE (Journal of Biological Chemistry (2010) 285, (22882-22889)).
Journal of Biological Chemistry, 286 (33).
p. 29442.
ISSN 0021-9258
Schmidt, Christoph S., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Baggs, Elizabeth M.
(2011)
Constraining the conditions conducive to dissimilatory nitrate reduction to ammonium in temperate arable soils.
Soil Biology and Biochemistry, 43 (7).
pp. 1607-1611.
ISSN 0038-0717
Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Edwards, Marcus J., Gates, Andrew J.
ORCID: https://orcid.org/0000-0002-4594-5038, Hall, Andrea, White, Gaye F., Bradley, Justin, Reardon, Catherine L., Shi, Liang, Beliaev, Alexander S., Marshall, Matthew J., Wang, Zheming, Watmough, Nicholas J., Fredrickson, James K., Zachara, John M., Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226 and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2011)
Structure of a bacterial cell surface decaheme electron conduit.
Proceedings of the National Academy of Sciences, 108 (23).
pp. 9384-9389.
ISSN 0027-8424
Gates, Andrew J. ORCID: https://orcid.org/0000-0002-4594-5038, Luque‑Almagro, Victor M., Goddard, Alan D., Ferguson, Stuart J., Roldán, M. Dolores and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2011)
A composite biochemical system for bacterial nitrate and nitrite assimilation as exemplified by Paracoccus denitrificans.
Biochemical Journal, 435 (3).
pp. 743-753.
ISSN 0264-6021
Cabrera, Juan J., Sánchez, Cristina, Gates, Andrew J. ORCID: https://orcid.org/0000-0002-4594-5038, Bedmar, Eulogio J., Mesa, Socorro, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Delgado, María J.
(2011)
The nitric oxide response in plant-associated endosymbiotic bacteria.
Biochemical Society Transactions, 39 (6).
pp. 1880-1885.
ISSN 0300-5127
Debieux, Charles M., Dridge, Elizabeth J., Mueller, Claudia M., Splatt, Peter, Paszkiewicz, Konrad, Knight, Iona, Florance, Hannah, Love, John, Titball, Richard W., Lewis, Richard J., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butler, Clive S.
(2011)
A bacterial process for selenium nanosphere assembly.
Proceedings of the National Academy of Sciences, 108 (33).
pp. 13480-13485.
ISSN 0027-8424
Field, Sarah J., Roldan, M. Dolores, Marritt, Sophie J., Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Watmough, Nicholas J.
(2011)
Electron transfer to the active site of the bacterial nitric oxide reductase is controlled by ligand binding to heme b3.
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1807 (4).
pp. 451-457.
Gates, Andrew J. ORCID: https://orcid.org/0000-0002-4594-5038, Butler, Clive S., Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226
(2011)
Electrocatalytic reduction of nitrate and selenate by NapAB.
Biochemical Society Transactions, 39 (1).
pp. 236-242.
ISSN 0300-5127
Gates, Andrew J. ORCID: https://orcid.org/0000-0002-4594-5038, Kemp, Gemma L., To, Chun Yip, Mann, James, Marritt, Sophie J., Mayes, Andrew G., Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226
(2011)
The relationship between redox enzyme activity and electrochemical potential—cellular and mechanistic implications from protein film electrochemistry.
Physical Chemistry Chemical Physics, 13 (17).
pp. 7720-7731.
ISSN 1463-9076
Lockwood, Colin, Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Clarke, Thomas A.
ORCID: https://orcid.org/0000-0002-6234-1914 and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2011)
Molecular interactions between multihaem cytochromes: probing the protein–protein interactions between pentahaem cytochromes of a nitrite reductase complex.
Biochemical Society Transactions, 39 (1).
pp. 263-268.
ISSN 0300-5127
Lockwood, Colin W. J., Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226, Hemmings, Andrew M.
ORCID: https://orcid.org/0000-0003-3053-3134 and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2011)
Characterization of the active site and calcium binding in cytochromecnitrite reductases.
Biochemical Society Transactions, 39 (6).
pp. 1871-1875.
ISSN 0300-5127
Luque‑Almagro, Victor M., Gates, Andrew J. ORCID: https://orcid.org/0000-0002-4594-5038, Moreno‑Vivián, Conrado, Ferguson, Stuart J., Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Roldán, M. Dolores
(2011)
Bacterial nitrate assimilation: gene distribution and regulation.
Biochemical Society Transactions, 39 (6).
pp. 1838-1843.
ISSN 0300-5127
Martínez‑Espinosa, Rosa María, Cole, Jeffrey A., Richardson, David ORCID: https://orcid.org/0000-0002-6847-1832 and Watmough, Nick
(2011)
Enzymology and ecology of the nitrogen cycle.
Biochemical Society Transactions, 39 (1).
pp. 175-178.
ISSN 0300-5127
Sánchez, Cristina, Cabrera, Juan J., Gates, Andrew J. ORCID: https://orcid.org/0000-0002-4594-5038, Bedmar, Eulogio J., Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Delgado, María J.
(2011)
Nitric oxide detoxification in the rhizobia–legume symbiosis.
Biochemical Society Transactions, 39 (1).
pp. 184-188.
ISSN 0300-5127
Zafrilla, Basilio, Martínez‑Espinosa, Rosa María, Bonete, Maria José, Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Gates, Andrew J.
ORCID: https://orcid.org/0000-0002-4594-5038
(2011)
A haloarchaeal ferredoxin electron donor that plays an essential role in nitrate assimilation.
Biochemical Society Transactions, 39 (6).
pp. 1844-1848.
ISSN 0300-5127
Goddard, Alan D., Stevens, Julie M., Rao, Feng, Mavridou, Despoina A. I., Chan, Weelee, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Allen, James W. A. and Ferguson, Stuart J.
(2010)
c-Type Cytochrome biogenesis can occur via a natural Ccm system lacking CcmH, CcmG, and the heme-binding histidine of CcmE.
The Journal of Biological Chemistry, 285 (30).
pp. 22882-22889.
ISSN 1083-351X
Kemp, Gemma L., Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Marritt, Sophie J., Lockwood, Colin, Poock, Susannah R., Hemmings, Andrew M.
ORCID: https://orcid.org/0000-0003-3053-3134, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832, Cheesman, Myles R. and Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226
(2010)
Kinetic and thermodynamic resolution of the interactions between sulfite and the pentahaem cytochrome NrfA from Escherichia coli.
Biochemical Journal, 431 (1).
pp. 73-80.
ISSN 0264-6021
Lowe, Elisabeth C., Bydder, Sarah, Hartshorne, Robert S., Tape, Hannah L. U., Dridge, Elizabeth J., Debieux, Charles M., Paszkiewicz, Konrad, Singleton, Ian, Lewis, Richard J., Santini, Joanne M., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butler, Clive S.
(2010)
Quinol-cytochrome c oxidoreductase and cytochrome c4 mediate electron transfer during selenate respiration in Thauera selenatis.
Journal of Biological Chemistry, 285 (24).
pp. 18433-18442.
ISSN 0021-9258
Sánchez, Cristina, Gates, Andrew J. ORCID: https://orcid.org/0000-0002-4594-5038, Meakin, Georgina E., Uchiumi, Toshiki, Girard, Lourdes, Richardson, Daivd J.
ORCID: https://orcid.org/0000-0002-6847-1832, Bedmar, Eulogio J. and Delgado, María J.
(2010)
Production of nitric oxide and nitrosylleghemoglobin complexes in soybean nodules in response to flooding.
Molecular Plant-Microbe Interactions, 23 (5).
pp. 702-711.
ISSN 0894-0282
Simpson, Philippa J. L., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Codd, Rachel
(2010)
The periplasmic nitrate reductase in Shewanella: the resolution, distribution and functional implications of two NAP isoforms, NapEDABC and NapDAGHB.
Microbiology, 156 (2).
pp. 302-312.
ISSN 1350-0872
Hartshorne, Robert S., Reardon, Catherine L., Ross, Daniel, Nuester, Jochen, Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Gates, Andrew J.
ORCID: https://orcid.org/0000-0002-4594-5038, Mills, Paul C., Fredrickson, Jim K., Zachara, John M., Shi, Liang, Beliaev, Alex S., Marshall, Matthew J., Tien, Ming, Brantley, Susan, Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226 and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2009)
Characterization of an electron conduit between bacteria and the extracellular environment.
Proceedings of the National Academy of Sciences, 106 (52).
pp. 22169-22174.
ISSN 0027-8424
Ize, Bérengère, Coulthurst, Sarah J., Hatzixanthis, Kostas, Caldelari, Isabelle, Buchanan, Grant, Barclay, Elaine C., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Palmer, Tracy and Sargent, Frank
(2009)
Remnant signal peptides on non-exported enzymes: implications for the evolution of prokaryotic respiratory chains.
Microbiology, 155 (12).
pp. 3992-4004.
ISSN 1350-0872
Wexler, Margaret, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Bond, Philip L.
(2009)
Radiolabelled proteomics to determine differential functioning of Accumulibacter during the anaerobic and aerobic phases of a bioreactor operating for enhanced biological phosphorus removal.
Environmental Microbiology, 11 (12).
pp. 3029-3044.
ISSN 1462-2920
Shi, Liang, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Wang, Zheming, Kerisit, Sebastien N., Rosso, Kevin M., Zachara, John M. and Fredrickson, James K.
(2009)
The roles of outer membrane cytochromes of Shewanella and Geobacterin extracellular electron transfer.
Environmental Microbiology Reports, 1 (4).
pp. 220-227.
ISSN 1758-2229
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Felgate, Heather, Watmough, Nick, Thomson, Andrew and Baggs, Elizabeth
(2009)
Mitigating release of the potent greenhouse gas N2O from the nitrogen cycle – could enzymic regulation hold the key?
Trends in Biotechnology, 27.
pp. 288-297.
ISSN 1879-3096
Bueno, Emilio, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Bedmar, Eulogio J. and Delgado, María J.
(2009)
Expression of Bradyrhizobium japonicum cbb(3) terminal oxidase under denitrifying conditions is subjected to redox control.
FEMS Microbiology Letters, 298 (1).
pp. 20-28.
ISSN 1574-6968
Pintathong, Punyawatt, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Spiro, Stephen and Choorit, Wanna
(2009)
Influence of metal ions and organic carbons on denitrification activity of the halotolerant bacterium, Paracoccus pantotrophus P16 a strain from shrimp pond.
Electronic Journal of Biotechnology, 12.
ISSN 0717-3458
Prior, K., Hautefort, I., Hinton, J. C. D., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832 and Rowley, G.
ORCID: https://orcid.org/0000-0002-5421-4333
(2009)
All stressed out. Salmonella pathogenesis and reactive nitrogen species.
Advances in Microbial Physiology, 56.
pp. 1-28.
Watmough, Nicholas J., Field, Sarah J., Hughes, Ross J. L. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
(2009)
The bacterial respiratory nitric oxide reductase.
Biochemical Society Transactions, 37.
pp. 392-399.
ISSN 1470-8752
Buchanan, Grant, Maillard, Julien, Nabuurs, Sander B., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Palmer, Tracy and Sargent, Frank
(2008)
Features of a twin-arginine signal peptide required for recognition by a Tat proofreading chaperone.
FEBS Letters, 582 (29).
pp. 3979-3984.
ISSN 1873-3468
Goddard, Alan D., Moir, James W. B., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, Stuart J.
(2008)
Interdependence of two NarK domains in a fused nitrate/nitrite transporter.
Molecular Microbiology, 70 (3).
pp. 667-681.
ISSN 1365-2958
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Thomson, Andrew J. and Watmough, Nicholas J.
(2008)
No laughing matter:The toxic gases of the nitrogen cycle.
Microbiology Today, 35 (3).
pp. 132-135.
ISSN 1464-0570
Bonete, Maria José, Martínez-Espinosa, Rosa María, Pire, Carmen, Zafrilla, Basilio and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
(2008)
Nitrogen metabolism in haloarchaea.
Saline Systems, 4.
ISSN 1746-1448
Donald, James W., Hicks, Matthew G., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Palmer, Tracy
(2008)
The c-type cytochrome OmcA localizes to the outer membrane upon heterologous expression in Escherichia coli.
Journal of Bacteriology, 190 (14).
pp. 5127-5131.
ISSN 1098-5530
van Wonderen, Jessica H., Burlat, Bénédicte, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Cheesman, Myles R. and Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226
(2008)
The nitric oxide reductase activity of cytochrome c nitrite reductase from Escherichia coli.
Journal of Biological Chemistry, 283 (15).
pp. 9587-9594.
ISSN 1083-351X
Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Kemp, Gemma L., Van Wonderen, Jessica H., Doyle, Rosie-Marie A. S., Cole, Jeffrey A., Tovell, Nick, Cheesman, Myles R., Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Hemmings, Andrew M.
ORCID: https://orcid.org/0000-0003-3053-3134
(2008)
Role of a conserved gluatmine residue in tuning the catalytic activity of Escherichia coli cytochrome c nitrite reductase.
Biochemistry, 47 (12).
pp. 3789-3799.
Flock, Ulrika, Thorndycroft, Faye H., Matorin, Andrey D., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Watmough, Nicholas J. and Adelroth, Pia
(2008)
Defining the proton entry point in the bacterial respiratory nitric oxide reductase.
Journal of Biological Chemistry, 283 (7).
pp. 3839-3845.
ISSN 1083-351X
Gates, Andrew J. ORCID: https://orcid.org/0000-0002-4594-5038, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226
(2008)
Voltammetric characterization of the aerobic energy-dissipating nitrate reductase of Paracoccus pantotrophus: exploring the activity of a redox-balancing enzyme as a function of electrochemical potential.
Biochemical Journal, 409 (1).
pp. 159-168.
ISSN 0264-6021
Bueno, Emilio, Bedmar, Eulogio J., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Delgado, María J.
(2008)
Role of Bradyrhizobium japonicum cytochrome c550 in nitrite and nitrate respiration.
FEMS Microbiology Letters, 279 (2).
pp. 188-194.
ISSN 1574-6968
Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Holley, Tracey, Hartshorne, Robert S., Fredrickson, Jim K., Zachara, John M., Shi, Liang and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2008)
The role of multihaem cytochromes in the respiration of nitrite in Eschericia coli and fe(III) in Shewanella oneidensis.
Biochemical Society Transactions, 36 (5).
pp. 1005-1010.
ISSN 1470-8752
Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Mills, Paul C., Poock, Susie R., Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226, Cheesman, Myles R., Cole, Jeffrey A., Hinton, Jay C. D., Hemmings, Andrew M.
ORCID: https://orcid.org/0000-0003-3053-3134, Kemp, Gemma, Söderberg, Christopher A. G., Spiro, Stephen, van Wonderen, Jessica and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2008)
Escherichia coli cytochrome c nitrite reductase NrfA.
Methods in Enzymology, 437.
pp. 63-77.
ISSN 1557-7988
Field, Sarah J., Thorndycroft, Faye H., Matorin, Andrey D., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Watmough, Nicholas J.
(2008)
The Paracoccus denitrificans respiratory NO reductase (NorBC).
Methods in Enzymology, 437.
pp. 79-101.
ISSN 1557-7988
Leaver, James T., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butler, Clive S.
(2008)
Enterobacter cloacae SLD1a-1 gains a selective advantage from selenate reduction when growing in nitrate-depleted anaerobic environments.
Journal of Industrial Microbiology and Biotechnology, 35 (8).
pp. 867-873.
ISSN 1476-5535
Mills, Paul C., Rowley, Gary ORCID: https://orcid.org/0000-0002-5421-4333, Spiro, S., Hinton, Jay C. D. and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2008)
A combination of cytochrome c nitrite reductase (NrfA) and flavorubredoxin (NorV) protects Salmonella enterica serovar Typhimurium against killing by NO in anoxic environments.
Microbiology, 154 (4).
pp. 1218-1228.
ISSN 1465-2080
Shi, Liang, Deng, Shuang, Marshall, Matthew J., Wang, Zheming, Kennedy, David W., Dohnalkova, Alice C., Mottaz, Heather M., Hill, Eric A., Gorby, Yuri A., Beliaev, Alexander S., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Zachara, John M. and Fredrickson, James K.
(2008)
Direct involvement of type II secretion system in extracellular translocation of Shewanella oneidensis outer membrane cytochromes MtrC and OmcA.
Journal of Bacteriology, 190 (15).
pp. 5512-5516.
ISSN 1098-5530
Simon, Jörg, van Spanning, Rob J. M. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
(2008)
The organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems.
Biochimica Et Biophysica Acta-Bioenergetics, 1777 (12).
pp. 1480-1490.
Martinez-Espinosa, Rosa María, Dridge, Elizabeth J., Bonete, Maria J., Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Butler, Clive S., Sargent, Frank and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2007)
Look on the positive side! The orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases.
FEMS Microbiology Letters, 276 (2).
pp. 129-139.
ISSN 1574-6968
Martinez-Espinosa, Rosa María, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226 and Bonete, María José
(2007)
Spectopotentiometric properties and salt-dependent thermotolerance of a [2Fe-2S] ferredoxin-involved nitrate assimilation in Haloferax mediterranei.
FEMS Microbiology Letters, 277 (1).
pp. 50-55.
ISSN 1574-6968
Hartshorne, Robert S., Jepson, Brian N., Clarke, Tom A. ORCID: https://orcid.org/0000-0002-6234-1914, Field, Sarah J., Fredrickson, Jim, Zachara, John, Shi, Liang, Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226 and Richardson, DJ
ORCID: https://orcid.org/0000-0002-6847-1832
(2007)
Characterization of Shewanella oneidensis MtrC: a cell-surface decaheme cytochrome involved in respiratory electron transport to extracellular electron acceptors.
JBIC Journal of Biological Inorganic Chemistry, 12 (7).
pp. 1083-1094.
ISSN 0949-8257
Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Cole, Jeffrey A., Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Hemmings, Andrew M.
ORCID: https://orcid.org/0000-0003-3053-3134
(2007)
The crystal structure of the pentahaem c-type cytochrome NrfB and characterization of its solution-state interaction with the pentahaem nitrite reductase NrfA.
Biochemical Journal, 406 (1).
pp. 19-30.
Hartshorne, Robert S., Kern, Melanie, Meyer, Björn, Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Karas, Michael, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Simon, Jörg
(2007)
A dedicated haem lyase is required for the maturation of a novel bacterial cytochrome c with unconventional covalent haem binding.
Molecular Microbiology, 64 (4).
pp. 1049-1060.
ISSN 0950-382X
Jepson, Brian J. N., Mohan, Sudesh, Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Gates, Andrew J.
ORCID: https://orcid.org/0000-0002-4594-5038, Cole, Jeffrey A., Butler, Clive S., Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226, Hemmings, Andrew M.
ORCID: https://orcid.org/0000-0003-3053-3134 and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2007)
Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli.
Journal of Biological Chemistry, 282 (9).
pp. 6425-6437.
ISSN 1083-351X
Thorndycroft, Faye H., Butland, Gareth, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Watmough, Nicholas J.
(2007)
A new assay for nitric oxide reductase reveals two conserved glutamate residues form the entrance to a proton-conducting channel in the bacterial enzyme.
Biochemical Journal, 401 (1).
pp. 111-119.
ISSN 0264-6021
Dridge, Elizabeth J., Watts, Carys A., Jepson, Brian J. N., Line, Kirsty, Santini, Joanne M., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butler, Clive S.
(2007)
Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy.
Biochemical Journal, 408 (1).
pp. 19-28.
Maillard, Julien, Spronk, Chris A. E. M., Buchanan, Grant, Lyall, Verity, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Palmer, Tracy, Vuister, Geerten W. and Sargent, Frank
(2007)
Structural diversity in twin-arginine signal peptide-binding proteins.
Proceedings of the National Academy of Sciences USA, 104 (40).
pp. 15641-15646.
ISSN 1091-6490
Meakin, Georgina E., Bueno, Emilio, Jepson, Brian, Bedmar, Eulogio J., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Delgado, María J.
(2007)
The contribution of bacteroidal nitrate and nitrite reduction to the formation of nitrosylleghaemoglobin complexes in soybean root nodules.
Microbiology, 153 (2).
pp. 411-419.
ISSN 1465-2080
Ross, Daniel E., Ruebush, Shane S., Brantley, Susan L., Hartshorne, Robert S., Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Tien, Ming
(2007)
Characterization of protein/protein interactions involved in iron reduction by Shewanella oneidensis MR-1.
Applied and Environmental Microbiology, 73.
pp. 5797-5808.
ISSN 1098-5336
Clarke, TA ORCID: https://orcid.org/0000-0002-6234-1914, Hemmings, AM
ORCID: https://orcid.org/0000-0003-3053-3134, Burlat, B, Butt, JN
ORCID: https://orcid.org/0000-0002-9624-5226, Cole, JA and Richardson, DJ
ORCID: https://orcid.org/0000-0002-6847-1832
(2006)
Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfovibrio desulfuricans.
Biochemical Society Transactions, 34 (1).
pp. 143-145.
ISSN 1470-8752
Dridge, E.J., Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832, Lewis, R.J. and Butler, C.S.
(2006)
Developing structure-based models to predict substrate specificity of D-group (Type II) molybdenum enzymes: Application to a molybdo-enzyme of unknown function from Archaeoglobus fulgidus.
Biochemical Society Transactions, 34.
pp. 118-121.
ISSN 1470-8752
Ellington, M.J., Fosdike, W.L., Sawers, R.G., Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, S.J.
(2006)
Regulation of the nap operon encoding the periplasmic nitrate reductase of Paracoccus pantotrophus: delineation of DNA sequences required for redox control.
Archives of Microbiology, 184 (5).
pp. 298-304.
Gwyer, J.D., Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butt, J.N.
ORCID: https://orcid.org/0000-0002-9624-5226
(2006)
Inhibiting Escherichia coli cytochrome c nitrite reductase: Voltammetry reveals an enzyme equipped for action despite the chemical challenges it may face in vivo.
Biochemical Society Transactions, 34 (1).
pp. 133-135.
ISSN 1470-8752
Hartshorne, S., Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832 and Simon, J.
(2006)
Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis.
Biochemical Society Transactions, 34.
pp. 146-149.
ISSN 1470-8752
Jepson, B. J. N., Marietou, A., Mohan, S., Cole, J. A., Butler, C. S. and Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832
(2006)
Evolution of the soluble nitrate reductase: defining the monomeric periplasmic nitrate reductase subgroup.
Biochemical Society Transactions, 34 (1).
pp. 122-126.
ISSN 1470-8752
Lam, Cathy K. S. Chung Chun, Jickells, Timothy D., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Russell, David A.
(2006)
Fluorescence-based siderophore biosensor for the determination of bioavailable iron in oceanic waters.
Analytical Chemistry, 78.
pp. 5040-5045.
ISSN 0003-2700
Lowe, E.C., Watts, C.A., Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832, Santini, J.M., Singleton, I. and Butler, C.S.
(2006)
The bioenergetics of selenate respiration in Thauera selenatis.
Biochimica et Biophysica Acta - Bioenergetics.
p. 203.
Martinez-Espinosa, R.M., Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832, Butt, J.N.
ORCID: https://orcid.org/0000-0002-9624-5226 and Bonete, M.J.
(2006)
Respiratory nitrate and nitrite pathway in the denitrifier haloarchaeon Haloferax mediterranei.
Biochemical Society Transactions, 34 (1).
pp. 115-117.
ISSN 1470-8752
Meakin, Georgina E., Jepson, Brian J. N., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Bedmar, Eulogio J. and Delgado, María J.
(2006)
The role of Bradyrhizobium japonicum nitric oxide reductase in nitric oxide detoxification in soya bean root nodules.
Biochemical Society Transactions, 34 (1).
pp. 195-196.
ISSN 1470-8752
Nilavongse, Arjaree, Brondijk, T. Harma C., Overton, Tim W., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Leach, Emily R. and Cole, Jeffrey A.
(2006)
The NapF protein of the Escherichia coli periplasmic nitrate reductase system: demonstration of a cytoplasmic location and interaction with the catalytic subunit, NapA.
Microbiology, 152.
pp. 3227-3237.
ISSN 1465-2080
Olmo-Mira, M. Francisca, Cabello, Purificación, Pino, Carmen, Martinez-Luque, Manuel, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Castillo, Francisco, Roldan, M. Dolores and Moreno-Vivian, Conrado
(2006)
Expression and characterization of the assimilatory NADH-nitrite reductase from the phototrophic bacterium Rhodobacter capsulatus E1F1.
Archives of Microbiology, 186 (4).
pp. 339-344.
Ridley, Helen, Watts, Carys A., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butler, Clive S.
(2006)
Resolution of distinct membrane-bound enzymes from Enterobacter cloacae SLD1a-1 that are responsible for selective reduction of nitrate and selenate oxyanions.
Applied and Environmental Microbiology, 72.
pp. 5173-5180.
ISSN 1098-5336
Ridley, Helen, Watts, Carys A., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butler, Clive S.
(2006)
Development of a viologen-based microtiter plate assay for the analysis of oxyanion reductase activity: Application to the membrane-bound selenate reductase from Enterobacter cloacae SLD1a-1.
Analytical Biochemistry, 358.
pp. 289-294.
ISSN 1096-0309
Southall, Stacey M., Doel, Justin J., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Oubrie, Arthur
(2006)
Soluble aldose sugar dehydrogenase from Escherichia coli - A highly exposed active site conferring broad substrate specificity.
Journal of Biological Chemistry, 281.
pp. 30650-30659.
ISSN 1083-351X
Gwyer, James D., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226
(2005)
Resolving complexity in the interactions of redox enzymes and their inhibitors: contrasting mechanisms for the inhibition of a cytochrome c nitrite reductase revealed by protein pilm voltammetry.
Biochemistry, 43 (47).
pp. 15086-15094.
Gwyer, James D., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226
(2005)
Diode or tunnel-diode characteristics? Resolving the catalytic consequences of proton coupled electron transfer in a multi-centered oxidoreductase.
Journal of the American Chemical Society, 127 (43).
pp. 14964-14965.
ISSN 0002-7863
Hatzixanthis, Kostas, Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Oubrie, Arthur, Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832, Turner, Raymond J. and Sargent, Frank
(2005)
Signal peptide-chaperone interactions on the twin-arginine protein transport pathway.
Proceedings of the National Academy of Sciences, 102.
pp. 8460-8465.
ISSN 0027-8424
Burlat, B., Gwyer, J. D., Poock, S., Clarke, T. A. ORCID: https://orcid.org/0000-0002-6234-1914, Cole, J. A., Hemmings, A. M.
ORCID: https://orcid.org/0000-0003-3053-3134, Cheesman, M. R., Butt, J. N.
ORCID: https://orcid.org/0000-0002-9624-5226 and Richardson, D. J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2005)
Cytochrome c nitrite reductase: from structural to physicochemical analysis.
Biochemical Society Transactions, 33 (1).
pp. 137-140.
ISSN 1470-8752
Butler, C.S. and Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832
(2005)
The emerging molecular structure of the nitrogen cycle: an introduction to the proceedings of the 10th annual N-cycle meeting.
Biochemical Society Transactions, 33.
pp. 113-118.
ISSN 1470-8752
Field, Sarah J., Thornton, Nicholas P., Anderson, Lee J., Gates, Andrew J. ORCID: https://orcid.org/0000-0002-4594-5038, Reilly, Ann, Jepson, Brian J. N., Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832, George, Simon J., Cheesman, Myles R. and Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226
(2005)
Reductive activation of nitrate reductases.
Dalton Transactions (21).
pp. 3580-3586.
ISSN 1477-9234
Hatzixanthis, K., Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832 and Sargent, F.
(2005)
Chaperones involved in assembly and export of N-oxide reductases.
Biochemical Society Transactions, 33 (1).
pp. 124-126.
ISSN 1470-8752
Li, Youguo, Wexler, Margaret, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Bond, Philip L. and Johnston, Andrew W. B.
(2005)
Screening a wide host-range, waste-water metagenomic library in tryptophan auxotrophs of Rhizobium leguminosarum and of Escherichia coli reveals different classes of cloned trp genes.
Environmental Microbiology, 7 (12).
pp. 1927-1936.
ISSN 1462-2920
Marietou, Angeliki, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Cole, Jeff and Mohan, Sudesh
(2005)
Nitrate reduction by Desulfovibrio desulfuricans: a periplasmic nitrate reductase system that lacks NapB, but includes a unique tetraheme c-type cytochrome, NapM.
FEMS Microbiology Letters, 248.
pp. 217-225.
ISSN 1574-6968
Mills, P. C., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832, Hinton, J. C. D. and Spiro, S.
(2005)
Detoxification of nitric oxide by the flavorubredoxin of Salmonella enterica serovar Typhimurium.
Biochemical Society Transactions, 33.
pp. 198-199.
ISSN 1470-8752
Watts, C.A., Ridley, H., Dridge, E.J., Leaver, J.T., Reilly, A.J., Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butler, C.S.
(2005)
Microbial reduction of selenate and nitrate: common themes and variations.
Biochemical Society Transactions, 33.
pp. 173-175.
ISSN 1470-8752
Wexler, Margaret, Bond, Philip L., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Johnston, Andrew W. B.
(2005)
A wide host-range metagenomic library from a waste water treatment plant yields a novel alcohol/aldehyde dehydrogenase that allows Rhizobium leguminosarum but not Escherichia coli to grow on ethanol.
Environmental Microbiology, 7 (12).
pp. 1917-1926.
ISSN 1462-2912
Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914, Dennison, Victoria, Seward, Harriet E., Burlat, Bénédicte, Cole, Jeffrey A., Hemmings, Andrew M.
ORCID: https://orcid.org/0000-0003-3053-3134 and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2004)
Purification and spectropotentiometric characterization of Escherichia coli NrfB, a decaheme homodimer that transfers electrons to the decaheme periplasmic nitrite reductase complex.
Journal of Biological Chemistry, 279 (40).
pp. 41333-41339.
ISSN 0021-9258
Jepson, Brian J. N., Anderson, Lee J., Rubio, Louis J., Taylor, Claire J., Butler, Clive S., Flores, Enrique, Herrero, Antonia, Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226 and Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832
(2004)
Tuning a nitrate reductase for function: The first spectropotentiometric characterization of a bacterial assimilatory nitrate reductase reveals novel redox properties.
The Journal of Biological Chemistry, 279 (31).
pp. 32212-32218.
ISSN 1083-351X
Brondijk, T. Harma C., Nilavongse, Arjaree, Filenko, Nina, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Cole, Jeffrey A.
(2004)
NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancing.
Biochemical Journal, 379 (1).
pp. 47-55.
Grönberg, Karin L. C., Watmough, Nicholas J., Thomson, Andrew J., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Field, Sarah J.
(2004)
Redox-dependent open and closed forms of the active site of the bacterial respiratory nitric-oxide reductase revealed by cyanide binding studies.
Journal of Biological Chemistry, 279 (17).
pp. 17120-17125.
ISSN 0021-9258
Gwyer, J, Angove, H, Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butt, Julea
ORCID: https://orcid.org/0000-0002-9624-5226
(2004)
Redox-triggered events in cytochrome c nitrite reductase.
Bioelectrochemistry, 63 (1-2).
pp. 43-47.
ISSN 1878-562X
Hedges, Duncan H. P., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Russell, David A.
(2004)
Electrochemical control of protein monolayers at indium tin oxide surfaces for the reagentless optical biosensing of nitric oxide.
Langmuir, 20 (5).
pp. 1901-1908.
Jormakka, Mika, Richardson, David ORCID: https://orcid.org/0000-0002-6847-1832, Byrne, Bernadette and Iwata, So
(2004)
Architecture of NarGH reveals a structural classification of Mo-bisMGD enzymes.
Structure, 12 (1).
pp. 95-104.
ISSN 1878-4186
Olmo-Mira, M. Francisca, Gavira, Mónica, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Castillo, Francisco, Moreno-Vivian, Conrado and Roldán, M. Dolores
(2004)
NapF is a cytoplasmic iron-sulfur protein required for Fe-S cluster assembly in the periplasmic nitrate reductase.
Journal of Biological Chemistry, 279.
pp. 49727-49735.
ISSN 1083-351X
Taylor, Clare J., Bain, Lindsey A., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Spiro, Stephen and Russell, David A.
(2004)
Construction of a whole-cell gene reporter for the fluorescent bioassay of nitrate.
Analytical Biochemistry, 328 (1).
pp. 60-66.
ISSN 1096-0309
Zajicek, Richard S., Allen, James W. A., Catron, Michaël L., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, Stuart J.
(2004)
Paracoccus pantotrophus NapC can reductively activate cytochrome cd(1) nitrite reductase.
FEBS Letters, 565.
pp. 48-52.
ISSN 1873-3468
Reyes-Ramirez, Francisca, Dobbin, Paul, Sawers, Gary and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
(2003)
Characterization of transcriptional regulation of Shewanella frigidimarina Fe(III)-induced flavocytochrome c reveals a novel iron-responsive gene regulation system.
Journal of Biological Chemistry, 185 (15).
pp. 4564-4571.
ISSN 1083-351X
Gates, Andrew J. ORCID: https://orcid.org/0000-0002-4594-5038, Hughes, Richard O., Sharp, Sarah R., Millington, Paul D., Nilavongse, Arjaree, Cole, Jeffrey A., Leach, Emily-Rose, Jepson, Brian J. N., Richardson, David J.
ORCID: https://orcid.org/0000-0002-6847-1832 and Butler, Clive S.
(2003)
Properties of the periplasmic nitrate reductases from Paracoccus pantotrophus and Escherichia coli after growth in tungsten-supplemented media.
FEMS Microbiology Letters, 220 (2).
pp. 261-269.
ISSN 1574-6968
Ellington, M.J.K., Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, S.J.
(2003)
Rhodobacter capsulatus gains a competitive advantage from respiratory nitrate reduction during light-dark transitions.
Microbiology, 149 (4).
pp. 941-948.
ISSN 1465-2080
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Characterisation of the expression and activity of the periplasmic nitrate reductase of Paracoccus pantotrophus in chemostat cultures.
Microbiology, 149 (6).
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Gregory, Lisa G., Bond, Philip L., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Spiro, Stephen
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Characterisation of a nitrate-respiring bacterial community using the nitrate reductase gene (NarG) as a functional marker.
Microbiology, 149.
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Pitts, Katy E., Dobbin, Paul S., Reyes-Ramirez, Francisca, Thomson, Andrew J., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Seward, Harriet E.
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Characterization of the Shewanella oneidensis MR-1 decaheme cytochrome MtrA: expression in Escherichia coli confers the ability to reduce soluble Fe(III) chelates.
Journal of Biological Chemistry, 278 (30).
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Watts, Carys A., Ridley, Helen, Condie, Kathryn L., Leaver, James T., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butler, Clive S.
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Selenate reduction by Enterobacter cloacae SLD1a-1 is catalysed by a molybdenum-dependent membrane-bound enzyme that is distinct from the membrane-bound nitrate reductase.
FEMS Microbiology Letters, 228 (2).
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Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Anderson, Lee J., Rubio, Luis M., Richardson, David J.
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Enzyme-catalysed nitrate reduction—themes and variations as revealed by protein film voltammetry.
Bioelectrochemistry, 56 (1-2).
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Angove, Hayley C., Cole, Jeffrey A., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Butt, Julea N.
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Protein film voltammetry reveals distinctive fingerprints of nitrite and hydroxylamine reduction by a cytochrome c nitrite reductase.
The Journal of Biological Chemistry, 277 (26).
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Spectral properties of bacterial nitric-oxide reductase: Resolution of pH-dependent forms of the active site heme b3.
The Journal of Biological Chemistry, 277 (23).
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Richardson, David ORCID: https://orcid.org/0000-0002-6847-1832 and Sawers, Gary
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Structural biology:PMF through the redox loop.
Science, 295 (5561).
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Structure and spectroscopy of the periplasmic cytochrome c nitrite reductase from Escherichia coli.
Biochemistry, 41 (9).
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Brondijk, T.H.C., Fiegen, D., Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832 and Cole, J.A.
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Roles of NapF, NapG and NapH, subunits of the Escherichia coli periplasmic nitrate reductase, in ubiquinol oxidation.
Molecular Microbiology, 44.
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Mo(V) co-ordination in the periplasmic nitrate reductase from Paracoccus pantotrophus probed by electron nuclear double resonance (ENDOR) spectroscopy.
Biochemical Journal, 363 (3).
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Butler, Clive S., Ferguson, Stuart J., Berks, Ben C., Thomson, Andrew J., Cheesman, Myles R. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
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Assignment of haem ligands and detection of electronic absorption bands of molybdenum in the di-haem periplasmic nitrate reductase of Paracoccus pantotrophus.
FEBS Letters, 500 (1-2).
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Protein film viltammetry of a respiratory nitrate reductase: evidence of complex electrochemical modulations of enzyme activity.
Journal of Inorganic Biochemistry, 86.
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Identification of two domains and distal histidine ligands to the four haems in the bacterial c-type cytochrome NapC; the prototype connector between quinol/quinone and periplasmic oxido-reductases.
Biochemical Journal, 368 (2).
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Elington, M. J. K., Bhakoo, K. K., Sawers, G., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, S. J.
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Hierarchy of carbon source selection in Paracoccus pantotrophus: Strict correlation between reduction state of the carbon substrate and aerobic expression of the nap operon.
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Properties of a soluble domain of subunit C of a bacterial nitric oxide reductase.
Biochemistry, 41 (35).
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Poock, Susannah R., Leach, Emily R., Moir, James W. B., Cole, Jeffrey A. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
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Respiratory detoxification of nitric oxide by the cytochrome c nitrite reductase of Escherichia coli.
Journal of Biological Chemistry, 277 (26).
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Magnetic circular dichroism spectroscopy of multiheme cytochromes involved in the iron respiration of Shewanella oneidensis.
Journal of Inorganic Biochemistry, 86.
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Two domains of a dual-function NarK protein are required for nitrate uptake, the first step of denitrification in Paracoccus pantotrophus.
Molecular Microbiology, 44 (1).
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Catalytic protein film voltammetry from a respiratory nitrate reductase provides evidence for complex electrochemical modulation of enzyme activity.
Biochemistry, 40 (38).
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Two conserved glutamates in the bacterial nitric oxide reductase are essential for activity but not assembley of the enzyme.
Journal of Bacteriology, 183 (1).
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Advances in Microbial Physiology, 45.
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Functional, biochemical and genetic diversity of prokaryotic nitrate reductases.
Cellular and Molecular Life Sciences, 58 (2).
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Introduction: nitrate reduction and the nitrogen cycle.
Cellular and Molecular Life Sciences, 58.
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Maximal expression of membrane-bound nitrate reductase in Paracoccus is induced by nitrate via a third FNR-like regulator named NarR.
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Thiocyanate binding to the molybdenum centre of the periplasmic nitrate reductase from Paracoccus pantotrophus.
Biochemical Journal, 352 (3).
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Bacterial respiration: a flexible process for a changing environment.
Microbiology, 146 (3).
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144th Meeting of the Society for General Microbiology, 1999 Fleming Lecture, 8 September 1999:Bacterial respiration: A flexible process for a changing environment.
Microbiology, 146 (3).
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Detection of genes for membrane-bound nitrate reductase in nitrate-respiring bacteria and in community DNA.
FEMS Microbiology Letters, 183 (2).
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Using direct electrochemistry to probe rate limiting events during nitrate reductase turnover.
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Voltammetry of a flavocytochrome c3:The lowest potential heme modulates fumarate reduction rates.
Biophysical Journal, 78 (2).
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Ferretti, Silvia, Lee, Sang-Kyung, MacCraith, Brian D., Oliva, Abel G., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Russell, David A., Sapsford, Kim E. and Vidal, Monica
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Optical biosensing of nitrite ions using cytochrome cd1 nitrite reductase encapsulated in a sol–gel matrix.
The Analyst, 125 (11).
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Ferretti, Silvia, Paynter, Sally, Russell, David A., Sapsford, Kim E. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
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Self-assembled monolayers: a versatile tool for the formulation of bio-surfaces.
TrAC Trends in Analytical Chemistry, 19 (9).
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Field, Sarah J., Dobbin, Paul S., Cheesman, Myles R., Watmough, Nicholas J., Thomson, Andrew J. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
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Purification and magneto-optical spectroscopic characterization of cytoplasmic membrane and outer membrane multiheme c-type cytochromes from Shewanella frigidimarina NCIMB400.
The Journal of Biological Chemistry, 275 (12).
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Sears, H. J., Sawers, G., Berks, B. C., Ferguson, S. J. and Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832
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Control of periplasmic nitrate reductase gene expression (napEDABC) from Paracoccus pantotrophus in response to oxygen and carbon substrates.
Microbiology, 146 (11).
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Grönberg, Karin L. C., Roldán, M. Dolores, Prior, Louise, Butland, Gareth, Cheesman, Myles R., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Spiro, Stephen, Thomson, Andrew J. and Watmough, Nicholas J.
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A low-redox potential heme in the dinuclear center of bacterial nitric oxide reductase: Implications for the evolution of energy-conserving heme−copper oxidases.
Biochemistry, 38 (42).
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Dobbin, Paul S., Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Powell, Anne K., Reid, Graeme A. and Richardson, David J.
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Characterization of a flavocytochrome that is induced during the anaerobic respiration of Fe3+ by Shewanella frigidimarina NCIMB400.
Biochemical Journal, 342 (2).
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Flanagan, Deborah A., Gregory, Lisa G., Carter, Jon P., Karakas-Sen, Asuman, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Spiro, Stephen
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Detection of genes for periplasmic nitrate reductase in nitrate respiring bacteria and in community DNA.
FEMS Microbiology Letters, 177 (2).
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Butler, Clive S., Charnock, John M., Bennett, Brian, Sears, Heather J., Reilly, Ann J., Ferguson, Stuart J., Garner, C. David, Lowe, David J., Thomson, Andrew J., Berks, Ben C. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
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Models for molybdenum coordination during the catalytic cycle of periplasmic nitrate reductase from Paracoccus denitrificans derived from EPR and EXAFS spectroscopy.
Biochemistry, 38 (28).
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Dobbin, Paul S., Carter, Jon P., San Juan, Carlos Garcia Salamanca, von Höbe, Marc, Powell, Anne K. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
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Dissimilatory Fe(III) reduction by Clostridium beijerinckii isolated from freshwater sediment using Fe(III) maltol enrichment.
FEMS Microbiology Letters, 176 (1).
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Bamford, Vicki, Dobbin, Paul S., Lee, Sor Cheng, Reilly, Ann, Powell, Anne K., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Hemmings, Andrew M.
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Crystallization and preliminary X-ray crystallographic analysis of a periplasmic tetrahaem flavocytochrome c3 from Shewanella frigidimarina NCIMB400 which has fumarate reductase activity.
Acta Crystallographica Section D: Biological Crystallography, 55 (6).
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Watmough, Nicholas J., Butland, Gareth, Cheesman, Myles R., Moir, James W. B., Richardson, David ORCID: https://orcid.org/0000-0002-6847-1832 and Spiro, Stephen
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Nitric oxide in bacteria: synthesis and consumption.
Biochimica Et Biophysica Acta-Bioenergetics, 1411 (2-3).
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Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Watmough, Nicholas J.
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Inorganic nitrogen metabolism in bacteria.
Current Opinion in Chemical Biology, 3 (2).
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Open conformation of a flavocytochrome c3 fumarate reductase.
Nature Structural Biology, 6 (12).
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Blyth, David J., Aylott, Jonathan W., Moir, James W.B., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Russell, David A.
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Optical biosensing of nitric oxide using the metalloprotein cytochrome c'.
Analyst, 124 (2).
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Roldan, M. Dolores, Sears, Heather J., Cheesman, Myles R., Ferguson, Stuart J., Thomson, Andrew J., Berks, Ben C. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
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Spectroscopic characterization of a novel multihemec-type Cytochrome widely implicated in bacterial electron transport.
Journal of Biological Chemistry, 273 (44).
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Crossman, Lisa C., Moir, James W. B., Spiro, Stephen and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
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Heterotrophic nitrification in Pamcoccus denitrificans.
Biochemical Society Transactions, 26 (3).
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The diversity of redox proteins involved in bacterial heterotrophic nitrification and aerobic denitrification.
Biochemical Society Transactions, 26 (3).
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Smith, Peter R., Holmes, Justin D., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Russell, David A. and Sodeau, John R.
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Photophysical and photochemical characterisation of bacterial semiconductor cadmium sulfide particles.
Journal of the Chemical Society - Faraday Transactions, 94 (9).
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Cheesman, Myles R., Ferguson, Stuart J., Moir, James W. B., Richardson, David ORCID: https://orcid.org/0000-0002-6847-1832, Zumft, Walter G. and Thomson, Andrew J.
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Two enzymes with a common function but different heme ligands in the forms as Isolated. Optical and magnetic properties of the heme groups in the oxidized forms of nitrite reductase, Cytochrome cd 1, from Pseudomonas stutzeri and Thiosphaera pantotropha.
Biochemistry, 36 (51).
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Crossman, Lisa C., Moir, James W.B., Enticknap, Julie J., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Spiro, Stephen
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Heterologous expression of heterotrophic nitrification genes.
Microbiology, 143 (12).
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Sears, Heather J., Spiro, Stephen and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
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Effect of carbon substrate and aeration on nitrate reduction and expression of the periplasmic and membrane-bound nitrate reductases in carbon-limited continuous cultures of Paracoccus denitrificans Pd1222.
Microbiology, 143 (12).
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Aylott, Jonathan W., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Russell, David A.
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Optical Biosensing of Gaseous Nitric Oxide Using Spin-Coated Sol - Gel Thin Films.
Chemistry of Materials, 9 (11).
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Holmes, Justin D., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Saed, Shaheen, Evans-Gowing, Richard, Russell, David A. and Sodeau, John R.
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Cadmium-specific formation of metal sulfide 'Q-particles' by Klebsiella pneumoniae.
Microbiology, 143 (8).
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Holmes, Justin D., Farrar, Jacqueline A., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Russell, David A. and Sodeau, John R.
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Bacterial cadmium sulfide semiconductor particles:An assessment of their photoactivity by EPR spectroscopy.
Photochemistry and Photobiology, 65 (5).
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Namiranian, Sholeh, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Russell, David A. and Sodeau, John R.
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Excited state properties of the siderophore pyochelin and its complex with zinc ions.
Photochemistry and Photobiology, 65 (5).
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Aylott, Jonathan W., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Russell, David A.
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Optical biosensing of nitrate ions using a sol-gel immobilized nitrate reductase.
Analyst, 122 (1).
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Identification of an assimilatory nitrate reductase in mutants of Paracoccus denitrificans GB17 deficient in nitrate respiration.
Archives of Microbiology, 167 (1).
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Moir, James W.B., Wehrfritz, Josa Marie, Spiro, Stephen and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
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The biochemical characterization of a novel non-haem-iron hydroxylamine oxidase from Paracoccus denitrificans GB17.
Biochemical Journal, 319 (3).
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Structural investigation of the molybdenum site of the periplasmic nitrate reductase from Thiosphaera pantotropha by X-ray absorption spectroscopy.
Biochemical Journal, 317 (2).
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Moir, James W.B., Crossman, Lisa C., Spiro, Stephen and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
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The purification of ammonia monooxygenase from Paracoccus denitrificans.
FEBS Letters, 387 (1).
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Dobbin, Paul S., Warren, Louise H., Cook, Nicola J., McEwan, Alastair G., Powell, Anne K. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
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Dissimilatory iron(III) reduction by rhodobacter capsulatus.
Microbiology, 142 (4).
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The influence of chelating agents upon the dissimilatory reduction of Fe(III) by Shewanella putrefaciens. Part 2. Oxo- and hydroxo-bridged polynuclear Fe(III) complexes.
BioMetals, 9 (3).
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Hydroxylamine oxidation in heterotrophic nitrate-reducing soil bacteria and purification of a hydroxylamine-cytochrome c oxidoreductase from a Pseudomonas species.
Archives of Microbiology, 166 (6).
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Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions.
BBA - Bioenergetics, 1232 (3).
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Bacterial photoprotection through extracellular cadmium sulfide crystallites.
Photochemistry and Photobiology, 62 (6).
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ISSN 0031-8655
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, Stuart J.
(1995)
Competition between hydrogen peroxide and nitrate for electrons from the respiratory chains of Thiosphaera pantotropha and Rhodobacter capsulatus.
FEMS Microbiology Letters, 132 (1-2).
pp. 125-129.
ISSN 0378-1097
Carter, J. P., Ya Hsin Hsiao, Hsin Hsiao, Spiro, S. and Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832
(1995)
Soil and sediment bacteria capable of aerobic nitrate respiration.
Applied and Environmental Microbiology, 61 (8).
pp. 2852-2858.
ISSN 0099-2240
Berks, B. C., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832, Reilly, A., Willis, A. C. and Ferguson, S. J.
(1995)
The napEDABC gene cluster encoding the periplasmic nitrate reductase system of Thiosphaera pantotropha.
Biochemical Journal, 309 (3).
pp. 983-992.
ISSN 0264-6021
Sears, H. J., Bennett, B., Spiro, S., Thomson, A. J. and Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832
(1995)
Identification of periplasmic nitrate reductase Mo(V) EPR signals in intact cells of Paracoccus denitrificans.
Biochemical Journal, 310 (1).
pp. 311-314.
ISSN 0264-6021
Moir, James W.B., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, Stuart J.
(1995)
The expression of redox proteins of denitrification in Thiosphaera pantotropha grown with oxygen, nitrate, and nitrous oxide as electron acceptors.
Archives of Microbiology, 164 (1).
pp. 43-49.
ISSN 0302-8933
Carter, Jon P., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Spiro, Stephen
(1995)
Isolation and characterisation of a strain of Pseudomonas putida that can express a periplasmic nitrate reductase.
Archives of Microbiology, 163 (3).
pp. 159-166.
ISSN 0302-8933
Holmes, Justin D., Smith, Peter R., Evans-Gowing, Richard, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Russell, David A. and Sodeau, John R.
(1995)
Energy-dispersive X-ray analysis of the extracellular cadmium sulfide crystallites of Klebsiella aerogenes.
Archives of Microbiology, 163 (2).
pp. 143-147.
ISSN 0302-8933
Berks, Ben C., Page, M. Dudley, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Reilly, Ann, Cavill, Alan, Outen, Fenno and Ferguson, Stuart J.
(1995)
Sequence analysis of subunits of the membrane‐bound nitrate reductase from a denitrifying bacterium:the integral membrane subunit provides a prototype for the dihaem electron‐carrying arm of a redox loop.
Molecular Microbiology, 15 (2).
pp. 319-331.
ISSN 0950-382X
Blyth, David J., Aylott, Jonathan W., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Russell, David A.
(1995)
Sol-gel encapsulation of metalloproteins for the development of optical biosensors for nitrogen monoxide and carbon monoxide.
The Analyst, 120 (11).
pp. 2725-2730.
ISSN 0003-2654
Bennett, Brian, Berks, Ben C., Ferguson, Stuart J., Thomson, Andrew J. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
(1994)
Mo(V) Electron Paramagnetic Resonance Signals from the Periplasmic Nitrate Reductase of Thiosphaera Pantotropha.
European Journal of Biochemistry, 226 (3).
pp. 789-798.
ISSN 0014-2956
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Bell, Louise C., Moir, James W.B. and Ferguson, Stuart J.
(1994)
A denitrifying strain of Rhodobacter capsulatus.
FEMS Microbiology Letters, 120 (3).
pp. 323-328.
ISSN 0378-1097
Breton, Jacques, Berks, Ben C., Reilly, Ann, Thomson, Andrew J., Ferguson, Stuart J. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
(1994)
Characterization of the paramagnetic iron-containing redox centres of Thiosphaera pantotropha periplasmic nitrate reductase.
FEBS Letters, 345 (1).
pp. 76-80.
ISSN 0014-5793
Berks, Ben C., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Robinson, Carol, Reilly, Ann, Aplin, Robin T. and Ferguson, Stuart J.
(1994)
Purification and characterization of the periplasmic nitrate reductase from Thiosphaera pantotropha.
European Journal of Biochemistry, 220 (1).
pp. 117-124.
ISSN 0014-2956
Wehrfritz, Josa Marie, Reilly, Ann, Spiro, Stephen and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832
(1993)
Purification of hydroxylamine oxidase from Thiosphaera pantotropha. Identification of electron acceptors that couple heterotrophic nitrification to aerobic denitrification.
FEBS Letters, 335 (2).
pp. 246-250.
ISSN 0014-5793
Sears, Heather J., Ferguson, Stuart J., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Spiro, Stephen
(1993)
The identification of a periplasmic nitrate reductase in Paracoccus denitrificans.
FEMS Microbiology Letters, 113 (1).
pp. 107-111.
ISSN 0378-1097
Berks, Ben C., Baratta, Daniela, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, Stuart J.
(1993)
Purification and characterization of a nitrous oxide reductase from Thiosphaera pantotropha Implications for the mechanism of aerobic nitrous oxide reduction.
European Journal of Biochemistry, 212 (2).
pp. 467-476.
ISSN 0014-2956
Moir, James W. B., Baratta, Daniela, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, Stuart J.
(1993)
The purification of a cd1‐type nitrite reductase from, and the absence of a copper‐type nitrite reductase from, the aerobic denitrifier Thiosphaera pantotropha; the role of pseudoazurin as an electron donor.
European Journal of Biochemistry, 212 (2).
pp. 377-385.
ISSN 0014-2956
Bell, L. C., Page, M. D., Berks, B. C., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, S. J.
(1993)
Insertion of transposon Tn5 into a structural gene of the membrane-bound nitrate reductase of Thiosphaera pantotropha results in anaerobic overexpression of periplasmic nitrate reductase activity.
Journal of General Microbiology, 139 (12).
pp. 3205-3214.
ISSN 0022-1287
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, Stuart J.
(1992)
The influence of carbon substrate on the activity of the periplasmic nitrate reductase in aerobically grown Thiosphaera pantotropha.
Archives of Microbiology, 157 (6).
pp. 535-537.
ISSN 0302-8933
Bell, L. C., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, S. J.
(1992)
Identification of nitric oxide reductase activity in Rhodobacter capsulatus:The electron transport pathway can either use or bypass both cytochrome c2 and the cytochrome bc1 complex.
Journal of General Microbiology, 138 (3).
pp. 437-443.
ISSN 0022-1287
McEwan, Alastair G., Benson, Neil, Bonnett, Tracey C., Hanlon, Steven P., Ferguson, Stuart J., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Jackson, J. Baz
(1991)
Bacterial dimethyl sulphoxide reductases and nitrate reductases.
Biochemical Society Transactions, 19 (3).
pp. 605-608.
ISSN 0300-5127
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Bell, Louise C., McEwan, Alastair G., Jackson, J. Baz and Ferguson, Stuart J.
(1991)
Cytochrome c2 is essential for electron transfer to nitrous oxide reductase from physiological substrates in Rhodobacter capsulatus and can act as an electron donor to the reductase in vitro Correlation with photoinhibition studies.
European Journal of Biochemistry, 199 (3).
pp. 677-683.
ISSN 0014-2956
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, McEwan, Alastair G., Page, M. Dudley, Jackson, J. Baz and Ferguson, Stuart J.
(1990)
The identification of cytochromes involved in the transfer of electrons to the periplasmic NO−3 reductase of Rhodobacter capsulatus and resolution of a soluble NO−3 ‐reductase − cytochrome‐c552 redox complex.
European Journal of Biochemistry, 194 (1).
pp. 263-270.
ISSN 0014-2956
Ballard, Anna L., McEwan, Alastair G., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Jackson, J. Baz and Ferguson, Stuart J.
(1990)
Rhodobacter capsulatus strain BK5 possesses a membrane bound respiratory nitrate reductase rather than the periplasmic enzyme found in other strains.
Archives of Microbiology, 154 (3).
pp. 301-303.
ISSN 0302-8933
Jones, M. R., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832, McEwan, A. G., Ferguson, S. J. and Jackson, J. B.
(1990)
In vivo redox poising of the cyclic electron transport system of Rhodobacter capsulatus and the effects of the auxiliary oxidants, nitrate, nitrous oxide and trimethylamine N-oxide, as revealed by multiple short flash excitation.
BBA - Bioenergetics, 1017 (3).
pp. 209-216.
ISSN 0005-2728
Bell, Louise C., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, Stuart J.
(1990)
Periplasmic and membrane-bound respiratory nitrate reductases in Thiosphaera pantotropha. The periplasmic enzyme catalyzes the first step in aerobic denitrification.
FEBS Letters, 265 (1-2).
pp. 85-87.
ISSN 0014-5793
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, McEwan, Alastair G., Jackson, J. Baz and Ferguson, Stuart J.
(1989)
Electron transport pathways to nitrous oxide in Rhodobacter species.
European Journal of Biochemistry, 185 (3).
pp. 659-669.
ISSN 0014-2956
McEwan, Alastair G., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Hudig, Hendrik, Ferguson, Stuart J. and Jackson, J. Barry
(1989)
Identification of cytochromes involved in electron transport to trimethylamine N-oxide/dimethylsulphoxide reductase in Rhodobacter capsulatus.
BBA - Bioenergetics, 973 (2).
pp. 308-314.
ISSN 0005-2728
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, King, Glenn F., Kelly, David J., McEwan, Alastair G., Ferguson, Stuart J. and Jackson, J. Barry
(1988)
Erratum: The role of auxiliary oxidants in maintaining redox balance during phototrophic growth of Rhodobacter capsulatuspropionate or butyrate.
Archives of Microbiology, 150 (6).
p. 602.
ISSN 0302-8933
Kelly, D. J., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832, Ferguson, S. J. and Jackson, J. B.
(1988)
Isolation of transposon Tn 5 insertion mutants of Rhodobacter capsulatus unable to reduce trimethylamine-N-oxide and dimethylsulphoxide.
Archives of Microbiology, 150 (2).
pp. 138-144.
ISSN 0302-8933
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, King, Glenn F., Kelly, David J., McEwan, Alastair G., Ferguson, Stuart J. and Jackson, J. Barry
(1988)
The role of auxiliary oxidants in maintaining redox balance during phototrophic growth of Rhodobacter capsulatus on propionate or butyrate.
Archives of Microbiology, 150 (2).
pp. 131-137.
ISSN 0302-8933
McEwan, A. G., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832, Jackson, J. B. and Ferguson, S. J.
(1988)
The periplasmic nitrate reductase and trimethylamine-N-oxide reductase of the photosynthetic bacterium Rhodobacter capsulatus.
Biochemical Society Transactions, 16 (2).
pp. 182-183.
ISSN 0300-5127
King, G. F., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832, Jackson, J. B. and Ferguson, S. J.
(1987)
Dimethylsulphoxide and trimethylamine-N-oxide as bacterial electron transport acceptors: Use of nuclear magnetic resonance to assay and characterise the reductase system in Rhodobacter capsulatus.
Archives of Microbiology, 149 (1).
pp. 47-51.
ISSN 0302-8933
Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832, Kelly, D. J., Jackson, J. B., Ferguson, S. J. and Alef, K.
(1986)
Inhibitory effects of myxothiazol and 2-n-heptyl-4-hydroxyquinoline-N-oxide on the auxiliary electron transport pathways of Rhodobacter capsulatus.
Archives of Microbiology, 146 (2).
pp. 159-165.
ISSN 0302-8933
Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832, Sawers, G. and Van Spanning, R. J. M.
(2021)
Bioenergetics theory and components:Periplasmic electron-transport systems in bacteria.
In:
Encyclopedia of Biological Chemistry.
Elsevier, pp. 31-37.
ISBN 9780128194607
Salas, Ana, Cabrera, Juan J., Jiménez-Leiva, Andrea, Mesa, Socorro, Bedmar, Eulogio J., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Gates, Andrew J.
ORCID: https://orcid.org/0000-0002-4594-5038 and Delgado, María J.
(2021)
Bacterial nitric oxide metabolism: recent insights in Rhizobia.
In:
Advances in Microbial Physiology.
Advances in Microbial Physiology, 78
.
Elsevier, pp. 259-315.
ISBN 9780128246016
Torregrosa-Crespo, Javier, Esclapez, Julia M., Bautista, Vanesa, Pire, Carmen, Gates, Andrew ORCID: https://orcid.org/0000-0002-4594-5038, Richardson, David
ORCID: https://orcid.org/0000-0002-6847-1832, Vegara, Anna, Camacho, Monica, Bonete, Maria José and Martínez‑Espinosa, Rosa María
(2018)
Denitrification in Extreme Environments.
In:
Extremophiles: From Biology to Biotechnology.
CRC Press.
ISBN 9781498774925
Lockwood, Colin, Van Wonderen, Jessica, Edwards, Marcus, Piper, Samuel, White, Gaye, Newton-Payne, Simone, Richardson, David ORCID: https://orcid.org/0000-0002-6847-1832, Clarke, Thomas
ORCID: https://orcid.org/0000-0002-6234-1914 and Butt, Julea
ORCID: https://orcid.org/0000-0002-9624-5226
(2018)
Membrane-Spanning Electron Transfer Proteins from Electrogenic Bacteria:Production and Investigation.
In:
Methods in Enzymology.
Elsevier, pp. 257-275.
Torregrosa-Crespo, J., Martínez-Espinosa, R. M., Esclapez, J., Bautista, V., Pire, C., Camacho, M., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832 and Bonete, M.J.
(2016)
Anaerobic Metabolism in Haloferax Genus: Denitrification as Case of Study.
In:
Advances in Microbial Physiology.
Elsevier, pp. 41-85.
ISBN 978-0-12-804822-1
White, Gaye F., Edwards, Marcus J., Gomez-Perez, Laura, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Butt, Julea N.
ORCID: https://orcid.org/0000-0002-9624-5226 and Clarke, Thomas A.
ORCID: https://orcid.org/0000-0002-6234-1914
(2016)
Mechanisms of Bacterial Extracellular Electron Exchange.
In:
Advances in Microbial Physiology.
Elsevier, pp. 87-138.
ISBN 978-0-12-804822-1
Butt, Julea ORCID: https://orcid.org/0000-0002-9624-5226, Gates, Andrew
ORCID: https://orcid.org/0000-0002-4594-5038, Marritt, Sophie and Richardson, David
ORCID: https://orcid.org/0000-0002-6847-1832
(2015)
Enzyme Film Electrochemistry.
In:
Electrochemical Processes in Biological Systems.
Wiley, New Jersey, pp. 105-120.
ISBN 978-0-470-57845-2
Wexler, Margaret, Bond, Philip L., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Johnston, Andrew W.B.
(2011)
Functional Screening a Wide Host-Range Metagenomic Library from a Wastewater Treatment Plant Yields a Novel Alcohol/Aldehyde Dehydrogenase.
In:
Handbook of Molecular Microbial Ecology II.
Wiley, pp. 451-459.
ISBN 9780470647196
Wexler, M, Bond, PL, Richardson, DJ ORCID: https://orcid.org/0000-0002-6847-1832 and Johnston, AWB
(2011)
Functional screening of a wide host-range metagenomic library from a wastewater treatment plant yields a novel alcohol/aldehyde dehydrogease.
In:
Metagenomics and Different Habitats Handbook of Molecular Microbial Ecology.
Wiley.
ISBN 978-0-470-64719-6
Ferguson, Stuart J., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Van Spanning, Rob J.M.
(2007)
Biochemistry and Molecular Biology of Nitrification.
In:
Biology of the Nitrogen Cycle.
Elsevier, pp. 209-222.
ISBN 9780444528575
Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Van Spanning, Rob J.M. and Ferguson, Stuart J.
(2007)
The Prokaryotic Nitrate Reductases.
In:
Biology of the Nitrogen Cycle.
Elsevier, pp. 21-35.
ISBN 9780444528575
van Spanning, Rob J.M., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, Stuart J.
(2007)
Introduction to the Biochemistry and Molecular Biology of Denitrification.
In:
Biology of the Nitrogen Cycle.
Elsevier, pp. 3-20.
ISBN 9780444528575