Peroxide reductase activity of NADH dehydrogenase of an alkaliphilic Bacillus in the presence of a 22-kDa protein component from Amphibacillus xylanus

被引：8

作者：

Koyama, N ^{[1
]}

Koitabashi, T

Niimura, Y

Massey, V

机构：

[1] Chiba Univ, Fac Sci, Dept Chem, Chiba 2638522, Japan

[2] Tokyo Univ Agr, Dept Food Sci & Technol, Abashiri, Hokkaido 0932422, Japan

[3] Univ Michigan, Sch Med, Dept Biol Chem, Ann Arbor, MI 48109 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 247卷 / 03期

关键词：

D O I：

10.1006/bbrc.1998.8749

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：

The NADH oxidase of Amphibacillus xylanus shows high NADH-peroxide reductase activity for hydrogen peroxide and alkyl hydroperoxides in the presence of a 22-kDa disulfide-containing protein component (Y. Niimura, L. B. Poole, and V. Massey, J.Biol.Chem. 270, 25645-25650, 1995). It was found that the membrane-bound NADH dehydrogenase of an alkaliphilic Bacillus (YN-1) involved in the respiratory chain also exhibits reductase activity for hydrogen peroxide and cumene hydroperoxide in the presence of the 22-kDa component from Amphibacillus xylanus. Vmax values for these substrates were as high as those of the NADH oxidase of A. xylanus. Although the 38-kDa protein produced by trypsin treatment of NADH dehydrogenase retains NADH dehydrogenase activity, it exhibited no peroxide reductase activity in the presence of the 22-kDa component from A. xylanus. The NADH dehydrogenase of YN-1 might not only catalyze electron flow from NADH to the respiratory chain, but also function for scavenging peroxide. (C) 1998 Academic Press.

引用

页码：659 / 662

页数：4

共 22 条

[11] AMPHIBACILLUS XYLANUS NADH OXIDASE AND SALMONELLA-TYPHIMURIUM ALKYL-HYDROPEROXIDE REDUCTASE FLAVOPROTEIN COMPONENTS SHOW EXTREMELY HIGH SCAVENGING ACTIVITY FOR BOTH ALKYL HYDROPEROXIDE AND HYDROGEN-PEROXIDE IN THE PRESENCE OF SALMONELLA-TYPHIMURIUM ALKYL-HYDROPEROXIDE REDUCTASE 22-KDA PROTEIN-COMPONENT [J].