An O2-inducible rubrerythrin-like protein, rubperoxin, is functional as a H2O2 reductase in an obligatory anaerobe Clostridium acetobutylicum

被引:16
作者
Kawasaki, Shinji [1 ]
Ono, Masaki [1 ]
Watamura, Yusuke [1 ]
Sakai, Yu [1 ]
Satoh, Takumi [1 ]
Arai, Toshiaki [1 ]
Satoh, Junichi [1 ]
Niimura, Youichi [1 ]
机构
[1] Tokyo Univ Agr, Dept Biosci, Setagaya Ku, Tokyo 1568502, Japan
来源
FEBS LETTERS | 2007年 / 581卷 / 13期
关键词
rubrerythrin; rubperoxin; hydrogen peroxide; peroxidase; clostridium acetobutylicum;
D O I
10.1016/j.febslet.2007.04.050
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
Clostridium acetobutylicum, an obligatory anaerobe, is able to grow microoxically with the accumulation of two functionally unknown O-2-induced proteins identified by two-dimensional electrophoresis. One was determined to be a novel type rubrerythrin-like protein, named rubperoxin (Rpr) in this study, that conserves one rubredoxin-type Fe(SCys)(4) Site per polypeptide in the N-terminus. Recombinant rubperoxin expressed in E. coli purified in its oxidized form is a dimer with optical absorption maxima at 492, 377, and 277 nm. Reduced rubperoxin is rapidly and fully oxidized by a half molar ratio of H2O2 per mole protein, and slowly oxidized by t-butyl hydroperoxide and O-2. Cell-free extracts from microoxically grown cells efficiently reduce rubperoxin when NAD(P)H is used as the electron donor (preferentially reduced by NADH). These results strongly suggest that rubperoxin is involved in NAD(P)H-dependent H2O2 detoxification in vivo. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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页码:2460 / 2464
页数:5
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