8RCC

W-formate dehydrogenase from Desulfovibrio vulgaris - aerobic soaked with 48 bar CO2 for 1 min

8RCC の概要

• エントリーDOI: 10.2210/pdb8rcc/pdb
• 関連するPDBエントリー: 8RC8 8RC9 8RCA 8RCB 8RCC
• 分子名称: Formate dehydrogenase, alpha subunit, selenocysteine-containing, CARBON DIOXIDE, OXYGEN MOLECULE, ... (12 entities in total)
• 機能のキーワード: formate, co2, molybdenum and tungsten enzymes, dmso reductase family, electron transport, oxidoreductase
• 由来する生物種: Nitratidesulfovibrio vulgaris str. Hildenborough; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 141253.31

構造登録者

Vilela-Alves, G.,Carpentier, P.,Manuel, R.R.,Pereira, I.C.,Romao, M.J.,Mota, C. (登録日: 2023-12-06, 公開日: 2024-07-24, 最終更新日: 2024-10-23)

主引用文献

Vilela-Alves, G.,Manuel, R.R.,Viegas, A.,Carpentier, P.,Biaso, F.,Guigliarelli, B.,Pereira, I.A.C.,Romao, M.J.,Mota, C.
Substrate-dependent oxidative inactivation of a W-dependent formate dehydrogenase involving selenocysteine displacement.
Chem Sci, 15:13090-13101, 2024

PubMed Abstract: Metal-dependent formate dehydrogenases are very promising targets for enzyme optimization and design of bio-inspired catalysts for CO reduction, towards innovative strategies for climate change mitigation. For effective application of these enzymes, the catalytic mechanism must be better understood, and the molecular determinants clarified. Despite numerous studies, several doubts persist, namely regarding the role played by the possible dissociation of the SeCys ligand from the Mo/W active site. Additionally, the oxygen sensitivity of these enzymes must also be understood as it poses an important obstacle for biotechnological applications. This work presents a combined biochemical, spectroscopic, and structural characterization of FdhAB (FdhAB) when exposed to oxygen in the presence of a substrate (formate or CO). This study reveals that O inactivation is promoted by the presence of either substrate and involves forming a different species in the active site, captured in the crystal structures, where the SeCys ligand is displaced from tungsten coordination and replaced by a dioxygen or peroxide molecule. This form was reproducibly obtained and supports the conclusion that, although W-FdhAB can catalyse the oxidation of formate in the presence of oxygen for some minutes, it gets irreversibly inactivated after prolonged O exposure in the presence of either substrate.

PubMed: 39148770
DOI: 10.1039/d4sc02394c

実験手法

X-RAY DIFFRACTION (2.301 Å)