7Z5O
W-formate dehydrogenase from Desulfovibrio vulgaris - Dithionite reduced form
This is a non-PDB format compatible entry.
Summary for 7Z5O
| Entry DOI | 10.2210/pdb7z5o/pdb |
| Descriptor | Formate dehydrogenase, alpha subunit, selenocysteine-containing, Formate dehydrogenase, beta subunit, putative, 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE, ... (10 entities in total) |
| Functional Keywords | formate, carbon dioxide, dithionite, oxidoreductase |
| Biological source | Desulfovibrio vulgaris str. Hildenborough More |
| Total number of polymer chains | 2 |
| Total formula weight | 142457.40 |
| Authors | Mota, C.,Oliveira, A.R.,Klymanska, K.,Pereira, I.C.,Romao, M.J. (deposition date: 2022-03-09, release date: 2022-07-13, Last modification date: 2024-11-13) |
| Primary citation | Oliveira, A.R.,Mota, C.,Klymanska, K.,Biaso, F.,Romao, M.J.,Guigliarelli, B.,Pereira, I.C. Spectroscopic and Structural Characterization of Reduced Desulfovibrio vulgaris Hildenborough W-FdhAB Reveals Stable Metal Coordination during Catalysis. Acs Chem.Biol., 17:1901-1909, 2022 Cited by PubMed Abstract: Metal-dependent formate dehydrogenases are important enzymes due to their activity of CO reduction to formate. The tungsten-containing FdhAB formate dehydrogenase from Hildenborough is a good example displaying high activity, simple composition, and a notable structural and catalytic robustness. Here, we report the first spectroscopic redox characterization of FdhAB metal centers by EPR. Titration with dithionite or formate leads to reduction of three [4Fe-4S] clusters, and full reduction requires Ti(III)-citrate. The redox potentials of the four [4Fe-4S] centers range between -250 and -530 mV. Two distinct W signals were detected, W and W, which differ in only the -value. This difference can be explained by small variations in the twist angle of the two pyranopterins, as determined through DFT calculations of model compounds. The redox potential of W was determined to be -370 mV when reduced by dithionite and -340 mV when reduced by formate. The crystal structure of dithionite-reduced FdhAB was determined at high resolution (1.5 Å), revealing the same structural alterations as reported for the formate-reduced structure. These results corroborate a stable six-ligand W coordination in the catalytic intermediate W state of FdhAB. PubMed: 35766974DOI: 10.1021/acschembio.2c00336 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.527 Å) |
Structure validation
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