Electron accepting units of the diheme cytochrome c TsdA, a bifunctional thiosulfate dehydrogenase/tetrathionate reductase

Kurth, Julia M., Brito, José A., Reuter, Jula, Flegler, Alexander, Koch, Tobias, Franke, Thomas, Klein, Eva-Maria, Rowe, Sam F., Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Denkmann, Kevin, Pereira, Ines A. C., Archer, Margarida and Dahl, Christiane (2016) Electron accepting units of the diheme cytochrome c TsdA, a bifunctional thiosulfate dehydrogenase/tetrathionate reductase. Journal of Biological Chemistry, 291. pp. 24804-24818. ISSN 0021-9258

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Abstract

The enzymes of the thiosulfate dehydrogenase (TsdA) family are wide-spread diheme c-type cytochromes. Here, redox carriers were studied mediating the flow of electrons arising from thiosulfate oxidation into respiratory or photosynthetic electron chains. In a number of organisms, including Thiomonas intermedia and Sideroxydans lithotrophicus the tsdA gene is immediately preceded by tsdB encoding for another diheme cytochrome. Spectrophotometric experiments in combination with enzymatic assays in solution showed that TsdB acts as an effective electron acceptor of TsdA in vitro when TsdA and TsdB originate from the same source organism. While TsdA covers a range from -300 mV to +150 mV, TsdB is redox active between -100 to +300 mV, thus enabling electron transfer between these hemoproteins. The three-dimensional structure of the TsdB-TsdA fusion protein from the purple sulfur bacterium Marichromatium purpuratum was solved by X-ray crystallography to 2.75 Å resolution providing insights into internal electron transfer. In the oxidized state, this tetraheme cytochrome c contains three hemes with axial His/Met ligation, while heme 3 exhibits the His/Cys coordination typical for TsdA active sites. Interestingly, thiosulfate is covalently bound to Cys330 on heme 3. In several bacteria including Allochromatium vinosum, TsdB is not present, precluding a general and essential role for electron flow. Both, AvTsdA and the MpTsdBA fusion react efficiently in vitro with high potential iron sulfur protein from A. vinosum (Em +350 mV). HiPIP not only acts as direct electron donor to the reaction center in anoxygenic phototrophs but can also be involved in aerobic respiratory chains.

Item Type:	Article
Uncontrolled Keywords:	crystal structure,cytochrome c,enzyme kinetics,heme,protein chemistry,respiratory chain,tsda,electron acceptor,thiosulfate dehydrogenase
Faculty \ School:	Faculty of Science > School of Chemistry Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Chemistry of Light and Energy Faculty of Science > Research Groups > Chemistry of Life Processes Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Energy Materials Laboratory
Depositing User:	Pure Connector
Date Deposited:	04 Oct 2016 12:02
Last Modified:	28 Oct 2023 01:02
URI:	https://ueaeprints.uea.ac.uk/id/eprint/60721
DOI:	10.1074/jbc.M116.753863

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