Purification and characterization of an NADH oxidase from Eubacterium ramulus

被引：12

作者：

Herles, C ^{[1
]}

Braune, A ^{[1
]}

Blaut, M ^{[1
]}

机构：

[1] Deutsch Inst Ernahrungsforsch, D-14558 Bergholz Rehbrucke, Germany

来源：

ARCHIVES OF MICROBIOLOGY | 2002年 / 178卷 / 01期

关键词：

NADH oxidase; Eubacterium ramulus;

D O I：

10.1007/s00203-002-0428-0

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

An NADH oxidase from the strictly anaerobic Eubacterium ramulus was purified to homogeneity. The enzyme is composed of two types of subunits with molecular masses of 40 and 30 kDa. The molecular mass of the native enzyme is 450 kDa according to gel filtration and PAGE analysis. Six to eight mol of FAD were found per mol of native enzyme. The NADH-specific enzyme was inhibited by N-bromosuccinimide and sulfhydryl reagents such as N-ethylmaleimide, CuCl2 or ZnCl2. The physiological function of the purified enzyme is unclear, but the demonstration of NADH-dependent O-2-consumption suggests that it plays a role in the scavenging of oxygen.

引用

页码：71 / 74

页数：4

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