4N4L

Kuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in hydrazine

4N4L の概要

• エントリーDOI: 10.2210/pdb4n4l/pdb
• 関連するPDBエントリー: 4N4J 4N4K 4N4M 4N4N 4N4O
• 分子名称: hydroxylamine oxidoreductase, PHOSPHATE ION, 1,2-ETHANEDIOL, ... (7 entities in total)
• 機能のキーワード: c-type cytochrome, oxidoreductase
• 由来する生物種: Candidatus Kuenenia stuttgartiensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 62715.54

構造登録者

Maalcke, W.J.,Dietl, A.,Marritt, S.J.,Butt, J.N.,Jetten, M.S.M.,Keltjens, J.T.,Barends, T.R.M.B.,Kartal, B. (登録日: 2013-10-08, 公開日: 2013-12-11, 最終更新日: 2024-10-09)

主引用文献

Maalcke, W.J.,Dietl, A.,Marritt, S.J.,Butt, J.N.,Jetten, M.S.,Keltjens, J.T.,Barends, T.R.,Kartal, B.
Structural Basis of Biological NO Generation by Octaheme Oxidoreductases.
J.Biol.Chem., 289:1228-1242, 2014

PubMed Abstract: Nitric oxide is an important molecule in all domains of life with significant biological functions in both pro- and eukaryotes. Anaerobic ammonium-oxidizing (anammox) bacteria that contribute substantially to the release of fixed nitrogen into the atmosphere use the oxidizing power of NO to activate inert ammonium into hydrazine (N2H4). Here, we describe an enzyme from the anammox bacterium Kuenenia stuttgartiensis that uses a novel pathway to make NO from hydroxylamine. This new enzyme is related to octaheme hydroxylamine oxidoreductase, a key protein in aerobic ammonium-oxidizing bacteria. By a multiphasic approach including the determination of the crystal structure of the K. stuttgartiensis enzyme at 1.8 Å resolution and refinement and reassessment of the hydroxylamine oxidoreductase structure from Nitrosomonas europaea, both in the presence and absence of their substrates, we propose a model for NO formation by the K. stuttgartiensis enzyme. Our results expand the understanding of the functions that the widespread family of octaheme proteins have.

PubMed: 24302732
DOI: 10.1074/jbc.M113.525147

実験手法

X-RAY DIFFRACTION (1.9 Å)