CRYSTAL-STRUCTURE OF THE NICKEL-IRON HYDROGENASE FROM DESULFOVIBRIO-GIGAS

被引：1345

作者：

VOLBEDA, A

CHARON, MH

PIRAS, C

HATCHIKIAN, EC

FREY, M

FONTECILLACAMPS, JC

机构：

[1] INST BIOL STRUCT,CRISTALLOG & CRISTALLOGENESE PROT LAB,F-38027 GRENOBLE 1,FRANCE

[2] CNRS,UNITE BIOENERGET & INGN PROT,F-13402 MARSEILLE 20,FRANCE

来源：

NATURE | 1995年 / 373卷 / 6515期

关键词：

D O I：

10.1038/373580a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The X-ray structure of the heterodimeric Ni-Fe hydrogenase from Desulfovibrio gigas, the enzyme responsible for the metabolism of molecular hydrogen, has been solved at 2.84 Angstrom resolution. The active site, which appears to contain, besides nickel, a second metal ion, is buried in the 60K subunit. The 28K subunit, which coordinates one [3Fe-4S] and two [4Fe-4S] clusters, contains an amino-terminal domain with similarities to the redox protein flavodoxin. The structure suggests plausible electron and proton transfer pathways.

引用

页码：580 / 587

页数：8

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[1] THE STRUCTURE AND MECHANISM OF IRON-HYDROGENASES [J].