Items where Research Group is "Centre for Molecular and Structural Biochemistry

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Number of items: 31.

Article

Aljabali, Alaa A. A., Barclay, J. Elaine, Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Lomonossoff, George P. and Evans, David J. (2010) Redox-active ferrocene-modified Cowpea mosaic virus nanoparticles. Dalton Transactions, 39 (32). pp. 7569-7574. ISSN 1477-9234

Bradshaw, David S. ORCID: https://orcid.org/0000-0002-6458-432X, Peck, Jamie N. T., Oganesyan, Vasily S. ORCID: https://orcid.org/0000-0002-8738-1146 and Andrews, David L. (2010) Optically controlled energy transfer in stacked and coplanar polycyclic chromophores. The Journal of Physical Chemistry Letters, 1 (18). pp. 2705-2708. ISSN 1948-7185

Girvan, Hazel M., Levy, Colin W., Williams, Paul, Fisher, Karl, Cheesman, Myles R., Rigby, Stephen E. J., Leys, David and Munro, Andrew W. (2010) Glutamate-haem ester bond formation is disfavoured in flavocytochrome P450 BM3: characterization of glutamate substitution mutants at the haem site of P450 BM3. Biochemical Journal, 427. pp. 455-466. ISSN 0264-6021

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

Gorna, Alina E., Bowater, Richard P. ORCID: https://orcid.org/0000-0002-2745-7807 and Dziadek, Jaroslaw (2010) DNA repair systems and the pathogenesis of Mycobacterium tuberculosis: varying activities at different stages of infection. Clinical Science, 119 (5). pp. 187-202. ISSN 0143-5221

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

Kirkwood, Mark, Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061, Todd, Jonathan D. and Johnston, Andrew W. B. (2010) The ddP gene of Roseovarius nubinhibens encodes a novel lyase that cleaves dimethylsulfoniopropionate into acrylate plus dimethyl sulfide. Microbiology, 156 (6). pp. 1900-1906. ISSN 1465-2080

Kirkwood, Mark, Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061, Todd, Jonathan D. and Johnston, Andrew W. B. (2010) The dddP gene of Roseovarius nubinhibens encodes a novel lyase that cleaves dimethylsulfoniopropionate into acrylate plus dimethyl sulfide. Microbiology, 156 (6). pp. 1900-1906. ISSN 1350-0872

Kuprusevicius, Egidisus, Edge, Ruth, Gopee, Hemant, Cammidge, Andrew N. ORCID: https://orcid.org/0000-0001-7912-4310, McInnes, Eric J. L., Wilson, Mark R. and Oganesyan, Vasily S. ORCID: https://orcid.org/0000-0002-8738-1146 (2010) Prediction of EPR spectra of liquid crystals with doped spin probes from fully atomistic molecular dynamics simulations: Exploring molecular order and dynamics at the phase transition. Chemistry - A European Journal, 16 (38). pp. 11558-11562. ISSN 0947-6539

Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061, Crow, Allister, Murphy, Michael E. P., Mauk, A. Grant and Moore, Geoffrey R. (2010) Iron core mineralisation in prokaryotic ferritins. Biochimica et Biophysica Acta, 1800 (8). pp. 732-744. ISSN 0006-3002

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

MacMillan, Fraser ORCID: https://orcid.org/0000-0002-2410-4790 and Hunte, Carola (2010) Quinone binding and catalysis:Preface. Biochimica Et Biophysica Acta-Bioenergetics, 1797 (12). p. 1841. ISSN 0005-2728

MacMillan, Fraser ORCID: https://orcid.org/0000-0002-2410-4790, Lange, Christian, Bawn, Matt and Hunte, Carola (2010) Resolving the EPR Spectra in the Cytochrome bc (1) Complex from Saccharomyces cerevisiae. Applied Magnetic Resonance, 37 (1-4). pp. 305-316. ISSN 0937-9347

Macmillan, Fraser ORCID: https://orcid.org/0000-0002-2410-4790, van Wonderen, Jessica, Cheesman, Myles, van der Hocht, Iris, Angerer, Heike, Gennis, Robert and Michel, Hartmut (2010) Using EPR up close and from afar: Elucidating mechanisms in haem copper oxidases. Biochimica Et Biophysica Acta-Bioenergetics, 1797. p. 97. ISSN 0005-2728

McMaster, Jonathan and Oganesyan, Vasily S. ORCID: https://orcid.org/0000-0002-8738-1146 (2010) Magnetic circular dichroism spectroscopy as a probe of the structures of the metal sites in metalloproteins. Current Opinion in Structural Biology, 20 (5). pp. 615-622.

Oganesyan, Vasily ORCID: https://orcid.org/0000-0002-8738-1146, White, Gaye, Field, Sarah, Marritt, Sophie, Gennis, Robert B., Yap, Lai Lai and Thomson, Andrew J. (2010) Nitroxide spin labels as EPR reporters of the relaxation and magnetic properties of the heme–copper site in cytochrome bo 3, E. coli. JBIC Journal of Biological Inorganic Chemistry, 15 (8). pp. 1255-1264. ISSN 0949-8257

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

Singleton, Chloe, White, Gaye F., Todd, Jonathan D., Marritt, Sophie J., Cheesman, Myles R., Johnston, Andrew W. B. and Le Brun, N ORCID: https://orcid.org/0000-0001-9780-4061 (2010) Heme-responsive DNA binding by the global iron regulator Irr from Rhizobium leguminosarum. The Journal of Biological Chemistry, 285 (21). pp. 16023-16031. ISSN 1083-351X

Smith, Laura J., Stapleton, Melanie R., Fullstone, Gavin J. M., Crack, Jason C., Thomson, Andrew J., Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061, Hunt, Debbie M., Harvey, Evelyn, Adinolfi, Salvatore, Buxton, Roger S. and Green, Jeffrey (2010) Mycobacterium tuberculosis WhiB1 is an essential DNA-binding protein with a nitric oxide sensitive iron-sulphur cluster. Biochemical Journal, 432 (3). pp. 417-427. ISSN 0264-6021

Stark, W. Marshall, Luisi, Ben F. and Bowater, Richard P. ORCID: https://orcid.org/0000-0002-2745-7807 (2010) Machines on genes: Enzymes that make, break and move DNA and RNA. Biochemical Society Transactions, 38 (2). pp. 381-383. ISSN 0300-5127

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

Todd, Jonathan D., Curson, Andrew R. J., Nikolaidou-Katsaraidou, Nefeli, Brearley, Charles A. ORCID: https://orcid.org/0000-0001-6179-9109, Watmough, Nicholas J., Chan, Yohan, Bulman Page, Philip C., Sun, Lei and Johnston, Andrew W. B. (2010) Molecular dissection of bacterial acrylate catabolism - unexpected links with dimethylsulfoniopropionate catabolism and dimethyl sulfide production. Environmental Microbiology, 12 (2). pp. 327-343. ISSN 1462-2920

Tucker, Nicholas P., Le Brun, Nick E. ORCID: https://orcid.org/0000-0001-9780-4061, Dixon, Ray and Hutchings, Matthew I. (2010) There's NO stopping NsrR, a global regulator of the bacterial NO stress response. Trends in Microbiology, 18 (4). pp. 149-156. ISSN 1878-4380

Turrell, Peter J., Wright, Joseph A. ORCID: https://orcid.org/0000-0001-9603-1001, Peck, Jamie N. T., Oganesyan, Vasily S. ORCID: https://orcid.org/0000-0002-8738-1146 and Pickett, Christopher J. (2010) The third hydrogenase: A ferracyclic carbamoyl with close structural analogy to the active site of Hmd. Angewandte Chemie-International Edition, 49 (41). pp. 7508-7511. ISSN 1433-7851

Watmough, Nicholas J. and Frerman, Frank E. (2010) The electron transfer flavoprotein: Ubiquinone oxidoreductases. Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1797 (12). pp. 1910-1916.

de Oliveira, Juliana Ferreira, Sforça, Maurício L., Blumenschein, Tharin ORCID: https://orcid.org/0000-0002-4932-5178, Goldfeder, Mauricio B., Guimarães, Beatriz G., Oliveira, Carla Columbano, Zanchin, Nilson I. T. and Zeri, Ana-Carolina (2010) Structure, dynamics, and RNA interaction analysis of the human SBDS protein. Journal of Molecular Biology, 396 (4). pp. 1053-1069. ISSN 1089-8638

von der Hocht, Iris, van Wonderen, Jessica H., MacMillan, Fraser ORCID: https://orcid.org/0000-0002-2410-4790 and Michel, Hartmut (2010) Interconversions of P and F intermediates of cytochrome c oxidase from Paracoccus denitrificans. Biochimica Et Biophysica Acta-Bioenergetics, 1797. p. 102. ISSN 0005-2728

Book Section

Cammack, Richard and MacMillan, Fraser ORCID: https://orcid.org/0000-0002-2410-4790 (2010) Applications of high resolution EPR to iron-sulphur proteins in electron transfer chains:Resolving complexity. In: Metals in Biology. Biological Magnetic Resonance . Springer, 11–44. ISBN 978-1-4419-1139-1

Cammack, Richard and MacMillan, Fraser ORCID: https://orcid.org/0000-0002-2410-4790 (2010) Electron Magnetic Resonance of Iron–Sulfur Proteins in Electron-Transfer Chains:Resolving Complexity. In: Metals in Biology. Springer, New York, NY, pp. 11-44. ISBN 978-1-4419-1138-4

MacMillan, Fraser ORCID: https://orcid.org/0000-0002-2410-4790 and Cammack, Richard (2010) Electron Magnetic Resonance of Iron-Sulfur Proteins in Electron-Transfer Chains:Resolving Complexity. In: Metals in Biology. Biological Magnetic Resonance, 29 . Springer-Verlag Berlin Heidelberg, pp. 11-44. ISBN 978-1-4419-1138-4

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