5OK4

Crystal structure of native [Fe]-hydrogenase Hmd from Methanothermobacter marburgensis inactivated by O2.

5OK4 の概要

• エントリーDOI: 10.2210/pdb5ok4/pdb
• 分子名称: 5,10-methenyltetrahydromethanopterin hydrogenase, FE (III) ION, 5'-O-[(S)-{[2-(carboxymethyl)-6-hydroxy-3,5-dimethylpyridin-4-yl]oxy}(hydroxy)phosphoryl]guanosine, ... (5 entities in total)
• 機能のキーワード: [fe]-hydrogenase, fe-guanylylpyridinol cofactor, h2, hydrogenase, methanogenesis, methenyl-tetrahydromethanopterin, methylene-tetrahydromethanopterin, hydrogenation, o2, inactivation, oxidoreductase
• 由来する生物種: Methanothermobacter marburgensis str. Marburg
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38494.97

構造登録者

Wagner, T.,Huang, G.,Bill, E.,Ermler, U.,Ataka, K.,Shima, S. (登録日: 2017-07-25, 公開日: 2018-05-16, 最終更新日: 2024-01-17)

主引用文献

Huang, G.,Wagner, T.,Ermler, U.,Bill, E.,Ataka, K.,Shima, S.
Dioxygen Sensitivity of [Fe]-Hydrogenase in the Presence of Reducing Substrates.
Angew. Chem. Int. Ed. Engl., 57:4917-4920, 2018

PubMed Abstract: Mono-iron hydrogenase ([Fe]-hydrogenase) reversibly catalyzes the transfer of a hydride ion from H to methenyltetrahydromethanopterin (methenyl-H MPT ) to form methylene-H MPT. Its iron guanylylpyridinol (FeGP) cofactor plays a key role in H activation. Evidence is presented for O sensitivity of [Fe]-hydrogenase under turnover conditions in the presence of reducing substrates, methylene-H MPT or methenyl-H MPT /H . Only then, H O is generated, which decomposes the FeGP cofactor; as demonstrated by spectroscopic analyses and the crystal structure of the deactivated enzyme. O reduction to H O requires a reductant, which can be a catalytic intermediate transiently formed during the [Fe]-hydrogenase reaction. The most probable candidate is an iron hydride species; its presence has already been predicted by theoretical studies of the catalytic reaction. The findings support predictions because the same type of reduction reaction is described for ruthenium hydride complexes that hydrogenate polar compounds.

PubMed: 29462510
DOI: 10.1002/anie.201712293

実験手法

X-RAY DIFFRACTION (1.29 Å)