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ToolsBennett, Brian, Charnock, John M., Sears, Heather J., Berks, Ben C., Thomson, Andrew J., Ferguson, Stuart J., Garner, C. David and Richardson, David J. (1996) Structural investigation of the molybdenum site of the periplasmic nitrate reductase from Thiosphaera pantotropha by X-ray absorption spectroscopy. Biochemical Journal, 317 (2). pp. 557-563. ISSN 0264-6021
Full text not available from this repository. (Request a copy)Abstract
The molybdenum centre of the periplasmic respiratory nitrate reductase from the denitrifying bacterium Thiosphaera pantotropha has been probed using molybdenum K-edge X-ray absorption spectroscopy. The optimum fit of the Mo(VI) EXAFS suggests two = O, three -S- and either a fourth -S- or an -O-/-N- as molybdenum ligands in the ferricyanide-oxidized enzyme. Three of the -S- ligands are proposed to be the two sulphur atoms of the molybdopterin dithiolene group and Cys-181. Comparison of the EXAFS of the ferricyanide-oxidized enzyme with that of a nitrate-treated sample containing 30% Mo(V) suggests that the Mo(VI) → Mo(V) reduction is accompanied by conversion of one = O to -O-. The best fit to the Mo(IV) EXAFS of dithionite-reduced enzyme was obtained using one = O, one -O- and four -S-/-Cl ligands. The periplasmic nitrate reductase molybdenum co-ordination environment in both the Mo(VI) and Mo(IV) oxidation states is distinct from that found in the membrane-bound respiratory nitrate reductase.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | biochemistry,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1303 |
| Faculty \ School: | Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 14 Jul 2022 17:30 |
| Last Modified: | 06 Feb 2025 10:40 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/86140 |
| DOI: | 10.1042/bj3170557 |
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