6N6P

Crystal structure of [FeFe]-hydrogenase in the presence of 7 mM Sodium dithionite

6N6P の概要

• エントリーDOI: 10.2210/pdb6n6p/pdb
• 関連するPDBエントリー: 6N59
• 分子名称: Iron hydrogenase 1, dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+), IRON/SULFUR CLUSTER, ... (6 entities in total)
• 機能のキーワード: [fefe]-hydrogenase, reactivity of [fefe]-hydrogenase, clostridium pasteurianum, iron sulfur clusters, electron-transfer, catalysis, oxidoreductase
• 由来する生物種: Clostridium pasteurianum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 66032.62

構造登録者

Zadvornyy, O.A.,Keable, S.M.,Peters, J.W. (登録日: 2018-11-26, 公開日: 2019-12-25, 最終更新日: 2023-10-11)

主引用文献

Artz, J.H.,Zadvornyy, O.A.,Mulder, D.W.,Keable, S.M.,Cohen, A.E.,Ratzloff, M.W.,Williams, S.G.,Ginovska, B.,Kumar, N.,Song, J.,McPhillips, S.E.,Davidson, C.M.,Lyubimov, A.Y.,Pence, N.,Schut, G.J.,Jones, A.K.,Soltis, S.M.,Adams, M.W.W.,Raugei, S.,King, P.W.,Peters, J.W.
Tuning Catalytic Bias of Hydrogen Gas Producing Hydrogenases.
J.Am.Chem.Soc., 142:1227-1235, 2020

PubMed Abstract: Hydrogenases display a wide range of catalytic rates and biases in reversible hydrogen gas oxidation catalysis. The interactions of the iron-sulfur-containing catalytic site with the local protein environment are thought to contribute to differences in catalytic reactivity, but this has not been demonstrated. The microbe produces three [FeFe]-hydrogenases that differ in "catalytic bias" by exerting a disproportionate rate acceleration in one direction or the other that spans a remarkable 6 orders of magnitude. The combination of high-resolution structural work, biochemical analyses, and computational modeling indicates that protein secondary interactions directly influence the relative stabilization/destabilization of different oxidation states of the active site metal cluster. This selective stabilization or destabilization of oxidation states can preferentially promote hydrogen oxidation or proton reduction and represents a simple yet elegant model by which a protein catalytic site can confer catalytic bias.

PubMed: 31816235
DOI: 10.1021/jacs.9b08756

実験手法

X-RAY DIFFRACTION (1.95 Å)