Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti

Jun Ye; Hung Chi Yang; Barry P. Rosen; Hiranmoy Bhattacharjee

doi:10.1016/j.febslet.2007.07.039

Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti

Jun Ye, Hung Chi Yang, Barry P. Rosen^*, Hiranmoy Bhattacharjee

^*此作品的通信作者

Wayne State University

研究成果: 期刊稿件 › 文章 › 同行評審

56 引文斯高帕斯（Scopus）

摘要

Purified ArsH from Sinorhizobium meliloti exhibits NADPH:FMN-dependent reduction of molecular O₂ to hydrogen peroxide and catalyzes reduction of azo dyes. The structure of ArsH was determined at 1.8 Å 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 β-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.

原文	英語
頁（從 - 到）	3996-4000
頁數	5
期刊	FEBS Letters
卷	581
發行號	21
DOIs	https://doi.org/10.1016/j.febslet.2007.07.039
出版狀態	已出版 - 21 08 2007
對外發佈	是

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title = "Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti",

abstract = "Purified ArsH from Sinorhizobium meliloti exhibits NADPH:FMN-dependent reduction of molecular O2 to hydrogen peroxide and catalyzes reduction of azo dyes. The structure of ArsH was determined at 1.8 {\AA} 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 β-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.",

keywords = "ArsH, Arsenic detoxification, Azoreductase, Flavoprotein, NADPH-FMN oxidoreductase",

author = "Jun Ye and Yang, {Hung Chi} and Rosen, {Barry P.} and Hiranmoy Bhattacharjee",

year = "2007",

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AU - Rosen, Barry P.

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PY - 2007/8/21

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AB - Purified ArsH from Sinorhizobium meliloti exhibits NADPH:FMN-dependent reduction of molecular O2 to hydrogen peroxide and catalyzes reduction of azo dyes. The structure of ArsH was determined at 1.8 Å 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 β-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.

KW - ArsH

KW - Arsenic detoxification

KW - Azoreductase

KW - Flavoprotein

KW - NADPH-FMN oxidoreductase

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SN - 0014-5793

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JF - FEBS Letters

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Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti

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