8BQL

W-formate dehydrogenase from Desulfovibrio vulgaris - Co-crystallized with Formate and Reoxidized by exposure to air for 12 min

8BQL の概要

• エントリーDOI: 10.2210/pdb8bql/pdb
• 分子名称: 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, ... (9 entities in total)
• 機能のキーワード: formate, co2, molybdenum and tungsten enzymes, dmso reductase family, oxidoreductase
• 由来する生物種: Desulfovibrio vulgaris str. Hildenborough; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 142546.65

構造登録者

Vilela-Alves, G.,Mota, C.,Oliveira, A.R.,Manuel, R.R.,Pereira, I.C.,Romao, M.J. (登録日: 2022-11-21, 公開日: 2023-01-18, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.906 Å)