PROPERTIES OF A THERMOSTABLE 4FE-FERREDOXIN FROM THE HYPERTHERMOPHILIC BACTERIUM THERMOTOGA-MARITIMA

被引：10

作者：

BLAMEY, JM

MUKUND, S

ADAMS, MWW

机构：

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

[2] UNIV GEORGIA,CTR METALLOENZYME STUDIES,ATHENS,GA 30602

来源：

FEMS MICROBIOLOGY LETTERS | 1994年 / 121卷 / 02期

关键词：

THERMOTOGA MARITIMA; FERMENTATION; THERMOSTABILITY; HYPERTHERMOPHILIC ARCHAEA; EVOLUTION;

D O I：

10.1016/0378-1097(94)90122-8

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A ferredoxin has been purified from one of the most ancient and most thermophilic bacteria known, Thermotoga maritima, which grows up to 90 degrees C. The reduced protein (M(r) approx. 6300) contains a single S = 1/2 [4Fe-4S](1+) cluster with complete cysteinyl ligation, and was unaffected after incubation at 95 degrees C for 12 h. It functioned as an electron carrier for T. maritima pyruvate oxidoreductase. Remarkably, the properties and amino acid sequence of this hyperthermophilic bacterial protein are much more similar to those of ferredoxins from hyperthermophilic archaea, rather than ferredoxins from mesophilic and moderately thermophilic bacteria.

引用

页码：165 / 169

页数：5

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