ALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM THE HYPERTHERMOPHILIC ARCHAEBACTERIUM PYROCOCCUS-FURIOSUS CONTAINS A TUNGSTEN OXO-THIOLATE CENTER

被引：66

作者：

GEORGE, GN

PRINCE, RC

MUKUND, S

ADAMS, MWW

机构：

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

[2] UNIV GEORGIA,CTR MET ENZYME STUDIES,ATHENS,GA 30602

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 1992年 / 114卷 / 09期

关键词：

D O I：

10.1021/ja00035a055

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

X-ray absorption spectroscopy has been used to characterize the tungsten site of the aldehyde ferredoxin oxidoreductase from the hyperthermophilic organism Pyrococcus furiosus. The enzyme contains a tungsten oxo-thiolate center, with two W = O at 1.74 angstrom, approximately three W-S- ligands at 2.41 angstrom, and (possibly) a W-O or W-N ligand at 2.1 angstrom. The tungsten site of this enzyme is structurally quite similar to that of molybdenum in the relatively well-known molybdenum oxo-thiolate enzymes.

引用

页码：3521 / 3523

页数：3

共 22 条

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