3TTB

Structure of the Thioalkalivibrio paradoxus cytochrome c nitrite reductase in complex with sulfite

3TTB の概要

• エントリーDOI: 10.2210/pdb3ttb/pdb
• 関連するPDBエントリー: 2OT4 3SXQ
• 分子名称: Eight-heme nitrite reductase, HEME C, SULFITE ION, ... (8 entities in total)
• 機能のキーワード: eight hemes c, nitrite reductase, oxidoreductase
• 由来する生物種: Thioalkalivibrio paradoxus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 129962.90

構造登録者

Polyakov, K.M.,Trofimov, A.A.,Tikhonova, T.V.,Tikhonov, A.V.,Dorovatovskii, P.V.,Popov, V.O. (登録日: 2011-09-14, 公開日: 2011-10-05, 最終更新日: 2024-11-27)

主引用文献

Tikhonova, T.,Tikhonov, A.,Trofimov, A.,Polyakov, K.,Boyko, K.,Cherkashin, E.,Rakitina, T.,Sorokin, D.,Popov, V.
Comparative structural and functional analysis of two octaheme nitrite reductases from closely related Thioalkalivibrio species.
Febs J., 279:4052-4061, 2012

PubMed Abstract: Octaheme nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio paradoxus was isolated and characterized. A comparative structural and functional analysis of two homologous octaheme nitrite reductases from closely related Thioalkalivibrio species was performed. It was shown that both enzymes have similar catalytic properties, owing to high structural similarity. Both enzymes are characterized by specific structural features distinguishing them from pentaheme cytochrome c nitrite reductases, such as the Tyr-Cys bond in the active site, the hexameric structure resulting in the formation of a void space inside the hexamer, and the product channel that opens into the void interior space of the hexamer. It is suggested that these specific structural features are responsible for the higher nitrite reductase activity, the greater preference for nitrite than for sulfite as a substrate, and the wider pH range of the catalytic activity of octaheme nitrite reductases than of pentaheme homologs.

PubMed: 22935005
DOI: 10.1111/j.1742-4658.2012.08811.x

実験手法

X-RAY DIFFRACTION (2 Å)