Recent structural insights into the function of copper nitrite reductases

被引:52
|
作者
Horrell, Sam [1 ]
Kekilli, Demet [1 ]
Strange, Richard W. [1 ]
Hough, Michael A. [1 ]
机构
[1] Univ Essex, Sch Biol Sci, Wivenhoe Pk, Colchester CO4 3SQ, Essex, England
基金
英国生物技术与生命科学研究理事会;
关键词
ALCALIGENES-FAECALIS S-6; X-RAY-STRUCTURE; ELECTRON-TRANSFER; ATOMIC-RESOLUTION; REDOX PARTNER; CRYSTAL-STRUCTURES; SUBSTRATE-BINDING; ACHROMOBACTER-CYCLOCLASTES; ORDERED MECHANISM; PROVIDE INSIGHT;
D O I
10.1039/c7mt00146k
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Copper nitrite reductases (CuNiR) carry out the first committed step of the denitrification pathway of the global nitrogen cycle, the reduction of nitrite (NO2-) to nitric oxide (NO). As such, they are of major agronomic and environmental importance. CuNiRs occur primarily in denitrifying soil bacteria which carry out the overall reduction of nitrate to dinitrogen. In this article, we review the insights gained into copper nitrite reductase (CuNiR) function from three dimensional structures. We particularly focus on developments over the last decade, including insights from serial femtosecond crystallography using X-ray free electron lasers (XFELs) and from the recently discovered 3-domain CuNiRs.
引用
收藏
页码:1470 / 1482
页数:13
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