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

Authors: Y, Montet; P, Amara; A, Volbeda; X, Vernede; E C, Hatchikian; M J, Field; M, Frey; +1 Authors

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

Abstract

The 2.54 A 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 H2 diffusion in the enzyme interior suggest that these channels serve as pathways for gas access to the active site.

Keywords

Models, Molecular, Binding Sites, Xenon, Protein Conformation, Crystallography, X-Ray, Structure-Activity Relationship, Hydrogenase, Computer Simulation, Desulfovibrio, Gases, Hydrogen

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Powered by OpenAIRE graph
citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
314
Top 10%
Top 1%
Top 10%