Observation of an unprecedented Cu bis-His site: Crystal structure of the H129V mutant of nitrite reductase

被引：9

作者：

Ellis, MJ

Antonyuk, SV

Strange, RW

Sawers, G

Eady, RR

Hasnain, SS ^{[1
]}

机构：

[1] CCLRC, Daresbury Lab, Mol Biophys Grp, Warrington WA4 4AD, Cheshire, England

[2] John Innes Ctr, Dept Mol Microbiol, Norwich NR4 7UH, Norfolk, England

[3] John Innes Ctr, Dept Biol Chem, Norwich NR4 7UH, Norfolk, England

来源：

INORGANIC CHEMISTRY | 2004年 / 43卷 / 24期

关键词：

D O I：

10.1021/ic048966p

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

Copper nitrite reductases contain both an electron-transfer type 1 Cu site and a catalytic type 2 Cu site. We have mutated one of the type 2 copper ligating histidines to observe the effect on catalytic turnover. This mutation has created a unique site where Cu is ligated by 2 His Nepsilon2 atoms alone.

引用

页码：7591 / 7593

页数：3

共 17 条

[1] PURIFICATION AND CHARACTERIZATION OF THE DISSIMILATORY NITRITE REDUCTASE FROM ALCALIGENES-XYLOSOXIDANS SUBSP XYLOSOXIDANS (NCIMB 11015) - EVIDENCE FOR THE PRESENCE OF BOTH TYPE-1 AND TYPE-2 COPPER CENTERS [J].