1QNI

Crystal Structure of Nitrous Oxide Reductase from Pseudomonas nautica, at 2.4A Resolution

1QNI の概要

• エントリーDOI: 10.2210/pdb1qni/pdb
• 分子名称: NITROUS-OXIDE REDUCTASE, DINUCLEAR COPPER ION, (MU-4-SULFIDO)-TETRA-NUCLEAR COPPER ION, ... (6 entities in total)
• 機能のキーワード: oxidoreductase, denitrification, mad, electron transfer
• 由来する生物種: PSEUDOMONAS NAUTICA
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 394554.76

構造登録者

Brown, K.,Tegoni, M.,Cambillau, C. (登録日: 1999-10-15, 公開日: 2000-10-13, 最終更新日: 2024-05-08)

主引用文献

Brown, K.,Tegoni, M.,Prudencio, M.,Pereira, A.S.,Besson, S.,Moura, J.J.,Moura, I.,Cambillau, C.
A novel type of catalytic copper cluster in nitrous oxide reductase.
Nat.Struct.Biol., 7:191-195, 2000

PubMed Abstract: Nitrous oxide (N20) is a greenhouse gas, the third most significant contributor to global warming. As a key process for N20 elimination from the biosphere, N20 reductases catalyze the two-electron reduction of N20 to N2. These 2 x 65 kDa copper enzymes are thought to contain a CuA electron entry site, similar to that of cytochrome c oxidase, and a CuZ catalytic center. The copper anomalous signal was used to solve the crystal structure of N20 reductase from Pseudomonas nautica by multiwavelength anomalous dispersion, to a resolution of 2.4 A. The structure reveals that the CuZ center belongs to a new type of metal cluster, in which four copper ions are liganded by seven histidine residues. N20 binds to this center via a single copper ion. The remaining copper ions might act as an electron reservoir, assuring a fast electron transfer and avoiding the formation of dead-end products.

PubMed: 10700275
DOI: 10.1038/73288

実験手法

X-RAY DIFFRACTION (2.4 Å)