2ZON

Crystal structure of electron transfer complex of nitrite reductase with cytochrome c

2ZON の概要

• エントリーDOI: 10.2210/pdb2zon/pdb
• 分子名称: Dissimilatory copper-containing nitrite reductase, cytochrome c551, COPPER (II) ION, ... (5 entities in total)
• 機能のキーワード: nitrite, electron transfer, denitrification, oxidoreductase-electron transport complex, oxidoreductase/electron transport
• 由来する生物種: Achromobacter xylosoxidans (Alcaligenes xylosoxidans); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 119470.38

構造登録者

Nojiri, M.,Koteishi, H.,Yamaguchi, K.,Suzuki, S. (登録日: 2008-05-27, 公開日: 2009-06-09, 最終更新日: 2023-11-01)

主引用文献

Nojiri, M.,Koteishi, H.,Nakagami, T.,Kobayashi, K.,Inoue, T.,Yamaguchi, K.,Suzuki, S.
Structural basis of inter-protein electron transfer for nitrite reduction in denitrification
Nature, 462:117-120, 2009

PubMed Abstract: Recent earth science studies have pointed out that massive acceleration of the global nitrogen cycle by anthropogenic addition of bio-available nitrogen has led to a host of environmental problems. Nitrous oxide (N(2)O) is a greenhouse gas that is an intermediate during the biological process known as denitrification. Copper-containing nitrite reductase (CuNIR) is a key enzyme in the process; it produces a precursor for N(2)O by catalysing the one-electron reduction of nitrite (NO2-) to nitric oxide (NO). The reduction step is performed by an efficient electron-transfer reaction with a redox-partner protein. However, details of the mechanism during the electron-transfer reaction are still unknown. Here we show the high-resolution crystal structure of the electron-transfer complex for CuNIR with its cognate cytochrome c as the electron donor. The hydrophobic electron-transfer path is formed at the docking interface by desolvation owing to close contact between the two proteins. Structural analysis of the interface highlights an essential role for the loop region with a hydrophobic patch for protein-protein recognition; it also shows how interface construction allows the variation in atomic components to achieve diverse biological electron transfers.

PubMed: 19890332
DOI: 10.1038/nature08507

実験手法

X-RAY DIFFRACTION (1.7 Å)