RUBREDOXIN OXIDASE, A NEW FLAVO-HEMO-PROTEIN, IS THE SITE OF OXYGEN REDUCTION TO WATER BY THE STRICT ANAEROBE DESULFOVIBRIO-GIGAS

被引：124

作者：

CHEN, L

LIU, MY

LEGALL, J

FARELEIRA, P

SANTOS, H

XAVIER, AV

机构：

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

[2] ESTACAO AGRON NACL,P-2780 OEIRAS,PORTUGAL

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 193卷 / 01期

关键词：

D O I：

10.1006/bbrc.1993.1595

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：

A rubredoxin-oxygen oxidoreductase, a homodimer with a molecular weight of 43 kDa per monomer, was found to be a component of an electron transfer chain that couples the reduction of oxygen to water with NADH oxidation. This FAD-containing protein appears to contain a new type of heme group. The electron transfer chain is not inhibited by cyanide and azide. In contrast, CO decreases NADH oxidation rate and also induces release of the prosthetic groups from the native terminal reductase. © 1993 Academic Press, Inc.

引用

页码：100 / 105

页数：6

共 11 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2] CALCIUM IS REQUIRED FOR THE REDUCTION OF SULFITE FROM HYDROGEN IN A RECONSTITUTED ELECTRON-TRANSFER CHAIN FROM THE SULFATE REDUCING BACTERIUM, DESULFOVIBRIO-GIGAS [J].