PURIFICATION, CHARACTERIZATION AND PROPERTIES OF AN NADH OXIDASE FROM DESULFOVIBRIO-VULGARIS (HILDENBOROUGH) AND ITS COUPLING TO ADENYLYL PHOSPHOSULFATE REDUCTASE

被引：23

作者：

CHEN, L

LEGALL, J

XAVIER, AV

机构：

[1] UNIV GEORGIA,DEPT BIOCHEM,ATHENS,GA 30602

[2] UNIV NOVA LISBOA,INST TECNOL QUIM & BIOL,P-2780 OEIRAS,PORTUGAL

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 203卷 / 02期

关键词：

D O I：

10.1006/bbrc.1994.2259

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：

An NADH oxidase was purified from Desulfovibrio vulgaris. This FMN-containing enzyme reacts with oxygen forming hydrogen peroxide with a specific activity of 0.21 mu moles.min(-1).mg(-1). The molecular weight of the protein was determined to be 65 kDa on 12.5% SDS/PAGE. It shows very low NADH: rubredoxin oxidoreductase activity specifically towards the rubredoxin from the same organism. However, adenylyl phosphosulfate reductase can be fully reduced by NADH with the purified enzyme,suggesting that NADH could be an electron donor for respiratory sulfate reduction. (C) 1994 Academic Press, Inc.

引用

页码：839 / 844

页数：6