8BQJ

W-formate dehydrogenase from Desulfovibrio vulgaris - Soaking with Formate 5 min

Summary for 8BQJ

• Entry DOI: 10.2210/pdb8bqj/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, co2, molybdenum and tungsten enzymes, dmso reductase family, oxidoreductase
• Biological source: Desulfovibrio vulgaris str. Hildenborough; More
• Total number of polymer chains: 2
• Total formula weight: 142438.56

Authors

Vilela-Alves, G.,Mota, C.,Oliveira, A.R.,Manuel, R.R.,Pereira, I.C.,Romao, M.J. (deposition date: 2022-11-21, release date: 2023-01-18, Last modification date: 2024-11-06)

Primary citation

Vilela-Alves, G.,Manuel, R.R.,Oliveira, A.R.,Pereira, I.C.,Romao, M.J.,Mota, C.
Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation.
Int J Mol Sci, 24:-, 2022

PubMed Abstract: Metal-dependent formate dehydrogenases (Fdh) catalyze the reversible conversion of CO to formate, with unrivalled efficiency and selectivity. However, the key catalytic aspects of these enzymes remain unknown, preventing us from fully benefiting from their capabilities in terms of biotechnological applications. Here, we report a time-resolved characterization by X-ray crystallography of the Hildenborough SeCys/W-Fdh during formate oxidation. The results allowed us to model five different intermediate structures and to chronologically map the changes occurring during enzyme reduction. Formate molecules were assigned for the first time to populate the catalytic pocket of a Fdh. Finally, the redox reversibility of FdhAB in crystals was confirmed by reduction and reoxidation structural studies.

PubMed: 36613918
DOI: 10.3390/ijms24010476

Experimental method

X-RAY DIFFRACTION (2.107 Å)