1YRQ

Structure of the ready oxidized form of [NiFe]-hydrogenase

1YRQ の概要

• エントリーDOI: 10.2210/pdb1yrq/pdb
• 関連するPDBエントリー: 1FRF 1YQW
• 分子名称: Periplasmic [NiFe] hydrogenase small subunit, Periplasmic [NiFe] hydrogenase large subunit, IRON/SULFUR CLUSTER, ... (8 entities in total)
• 機能のキーワード: nib state, hydroxide bridge, oxidoreductase
• 由来する生物種: Desulfovibrio fructosovorans; 詳細
• 細胞内の位置: Periplasm: P18187 P18188
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 535515.32

構造登録者

Volbeda, A.,Martin, L.,Cavazza, C.,Matho, M.,Faber, B.W.,Roseboom, W.,Albracht, S.P.,Garcin, E.,Rousset, M.,Fontecilla-Camps, J.C. (登録日: 2005-02-04, 公開日: 2005-04-19, 最終更新日: 2024-10-09)

主引用文献

Volbeda, A.,Martin, L.,Cavazza, C.,Matho, M.,Faber, B.W.,Roseboom, W.,Albracht, S.P.,Garcin, E.,Rousset, M.,Fontecilla-Camps, J.C.
Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases.
J.Biol.Inorg.Chem., 10:239-249, 2005

PubMed Abstract: [NiFe] hydrogenases catalyze the reversible heterolytic cleavage of molecular hydrogen. Several oxidized, inactive states of these enzymes are known that are distinguishable by their very different activation properties. So far, the structural basis for this difference has not been understood because of lack of relevant crystallographic data. Here, we present the crystal structure of the ready Ni-B state of Desulfovibrio fructosovorans [NiFe] hydrogenase and show it to have a putative mu-hydroxo Ni-Fe bridging ligand at the active site. On the other hand, a new, improved refinement procedure of the X-ray diffraction data obtained for putative unready Ni-A/Ni-SU states resulted in a more elongated electron density for the bridging ligand, suggesting that it is a diatomic species. The slow activation of the Ni-A state, compared with the rapid activation of the Ni-B state, is therefore proposed to result from the different chemical nature of the ligands in the two oxidized species. Our results along with very recent electrochemical studies suggest that the diatomic ligand could be hydro-peroxide.

PubMed: 15803334
DOI: 10.1007/s00775-005-0632-x

実験手法

X-RAY DIFFRACTION (2.1 Å)