Tools
Tools
Bennett, Brian, Charnock, John M., Sears, Heather J., Berks, Ben C., Thomson, Andrew J., Ferguson, Stuart J., Garner, C. David and Richardson, David J. 
ORCID: https://orcid.org/0000-0002-6847-1832
(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
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: | 15 May 2023 00:54 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/86140 |
| DOI: | 10.1042/bj3170557 |
Actions (login required)
 |
View Item |