Side-on copper-nitrosyl coordination by nitrite reductase

被引：202

作者：

Tocheva, EI

Rosell, FI

Mauk, AG

Murphy, MEP ^{[1
]}

机构：

[1] Univ British Columbia, Dept Microbiol & Immunol, Vancouver, BC V6T 1Z3, Canada

[2] Univ British Columbia, Dept Biochem & Mol Biol, Vancouver, BC V6T 1Z3, Canada

来源：

SCIENCE | 2004年 / 304卷 / 5672期

关键词：

D O I：

10.1126/science.1095109

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

A copper-nitrosyl intermediate forms during the catalytic cycle of nitrite reductase, the enzyme that mediates the committed step in bacterial denitrification. The crystal structure of a type 2 copper-nitrosyl complex of nitrite reductase reveals an unprecedented side-on binding mode in which the nitrogen and oxygen atoms are nearly equidistant from the copper cofactor. Comparison of this structure with a refined nitrite-bound crystal structure explains how coordination can change between copper-oxygen and copper-nitrogen during catalysis. The side-on copper-nitrosyl in nitrite reductase expands the possibilities for nitric oxide interactions in copper proteins such as superoxide dismutase and prions.

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页码：867 / 870

页数：4

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