Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics

被引：279
作者：
Montet, Y
Amara, P
Volbeda, A
Vernede, X
Hatchikian, EC
Field, MJ
Frey, M
FontecillaCamps, JC
机构：
[1] CEA, CNRS, INST BIOL STRUCT JP EBEL, CRISTALLOG & CRISTALLOGENESE PROT LAB, F-38027 GRENOBLE 1, FRANCE
[2] CEA, CNRS, INST BIOL STRUCT JP EBEL, LAB DYNAM MOL, F-38027 GRENOBLE 1, FRANCE
[3] CNRS, UNITE BIOENERGET & INGN PROT, F-13042 MARSEILLE 20, FRANCE
来源：
NATURE STRUCTURAL BIOLOGY | 1997年 / 4卷 / 07期
关键词：
D O I：
10.1038/nsb0797-523
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：
The 2.54 Angstrom resolution structure of Ni-Fe hydrogenase has revealed the existence of hydrophobic channels connecting the molecular surface to the active site. A crystallographic analysis of xenon binding together with molecular dynamics simulations of xenon and Hz diffusion in the enzyme interior suggest that these channels serve as pathways for gas access to the active site.
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页码：523 / 526
页数：4
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