4IUC

Crystal structure of an O2-tolerant [NiFe]-hydrogenase from Ralstonia eutropha in its as-isolated form - oxidized state 2

4IUC の概要

• エントリーDOI: 10.2210/pdb4iuc/pdb
• 関連するPDBエントリー: 4IUB 4IUD
• 分子名称: Uptake hydrogenase large subunit, Uptake hydrogenase small subunit, NI-FE OXIDIZED ACTIVE CENTER, ... (9 entities in total)
• 機能のキーワード: [nife] hydrogenase, knallgas bacteria, proteobacteria, aerobic hydrogen bacteria, hydrogen catalysis, metalloenzyme, metalloprotein catalytic center, nickel-iron cofactor, bimetallic, ni-fe active site, iron-sulfur cluster, [4fe-3s] cluster, [3fe-4s] cluster, [4fe-4s] cluster, reduced state, oxidized state, oxygen-tolerant hydrogenase, membrane-bound, oxidoreductase
• 由来する生物種: Ralstonia eutropha; 詳細
• 細胞内の位置: Cell membrane; Peripheral membrane protein: P31891 P31892
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 105920.52

構造登録者

Frielingsdorf, S.,Schmidt, A.,Fritsch, J.,Lenz, O.,Scheerer, P. (登録日: 2013-01-20, 公開日: 2014-04-02, 最終更新日: 2023-09-20)

主引用文献

Frielingsdorf, S.,Fritsch, J.,Schmidt, A.,Hammer, M.,Lowenstein, J.,Siebert, E.,Pelmenschikov, V.,Jaenicke, T.,Kalms, J.,Rippers, Y.,Lendzian, F.,Zebger, I.,Teutloff, C.,Kaupp, M.,Bittl, R.,Hildebrandt, P.,Friedrich, B.,Lenz, O.,Scheerer, P.
Reversible [4Fe-3S] cluster morphing in an O2-tolerant [NiFe] hydrogenase.
Nat.Chem.Biol., 10:378-385, 2014

PubMed Abstract: Hydrogenases catalyze the reversible oxidation of H(2) into protons and electrons and are usually readily inactivated by O(2). However, a subgroup of the [NiFe] hydrogenases, including the membrane-bound [NiFe] hydrogenase from Ralstonia eutropha, has evolved remarkable tolerance toward O(2) that enables their host organisms to utilize H(2) as an energy source at high O(2). This feature is crucially based on a unique six cysteine-coordinated [4Fe-3S] cluster located close to the catalytic center, whose properties were investigated in this study using a multidisciplinary approach. The [4Fe-3S] cluster undergoes redox-dependent reversible transformations, namely iron swapping between a sulfide and a peptide amide N. Moreover, our investigations unraveled the redox-dependent and reversible occurence of an oxygen ligand located at a different iron. This ligand is hydrogen bonded to a conserved histidine that is essential for H(2) oxidation at high O(2). We propose that these transformations, reminiscent of those of the P-cluster of nitrogenase, enable the consecutive transfer of two electrons within a physiological potential range.

PubMed: 24705592
DOI: 10.1038/nchembio.1500

実験手法

X-RAY DIFFRACTION (1.45 Å)