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

^*Corresponding author for this work

Wayne State University

Research output: Contribution to journal › Journal Article › peer-review

56 Scopus citations

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 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.

Original language	English
Pages (from-to)	3996-4000
Number of pages	5
Journal	FEBS Letters
Volume	581
Issue number	21
DOIs	https://doi.org/10.1016/j.febslet.2007.07.039
State	Published - 21 08 2007
Externally published	Yes

Keywords

ArsH
Arsenic detoxification
Azoreductase
Flavoprotein
NADPH-FMN oxidoreductase

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10.1016/j.febslet.2007.07.039

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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",

month = aug,

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doi = "10.1016/j.febslet.2007.07.039",

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T1 - Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti

AU - Ye, Jun

AU - Yang, Hung Chi

AU - Rosen, Barry P.

AU - Bhattacharjee, Hiranmoy

PY - 2007/8/21

Y1 - 2007/8/21

N2 - 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.

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

UR - https://www.scopus.com/pages/publications/34547652441

U2 - 10.1016/j.febslet.2007.07.039

DO - 10.1016/j.febslet.2007.07.039

M3 - 文章

C2 - 17673204

AN - SCOPUS:34547652441

SN - 0014-5793

VL - 581

SP - 3996

EP - 4000

JO - FEBS Letters

JF - FEBS Letters

IS - 21

ER -

Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti

Abstract

Keywords

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