Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti

被引：62

作者：

Ye, Jun ^{[1
]}

Yang, Hung-Chi ^{[1
]}

Rosen, Barry P. ^{[1
]}

Bhattacharjee, Hirannioy ^{[1
]}

机构：

[1] Wayne State Univ, Sch Med, Dept Biochem & Mol Biol, Detroit, MI 48201 USA

来源：

FEBS LETTERS | 2007年 / 581卷 / 21期

关键词：

ArsH; arsenic detoxification; flavoprotein; NADPH-FMN oxidoreductase; azoreductase;

D O I：

10.1016/j.febslet.2007.07.039

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：

Purified ArsH from Sinorhizobium meliloti exhibits NADPH:FMN-dependent reduction of molecular O-2 to hydrogen peroxide and catalyzes reduction of azo dyes. The structure of ArsH was determined at 1.8 angstrom resolution. ArsH crystallizes with eight molecules in the asymmetric unit forming two tetramers. Each monomer has a core domain with a central five-stranded parallel P-sheet and two monomers interact to form a classical flavodoxin-like dimer. The N- and C-terminal extensions of ArsH are involved in interactions between subunits and tetramer formation. The structure may provide insight in how ArsH participates in arsenic detoxification. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：3996 / 4000

页数：5

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