Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics
doi: 10.1038/nsb0797-523
pmid: 9228943
Gas access to the active site of Ni-Fe hydrogenases probed by X-ray crystallography and molecular dynamics
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.
Models, Molecular, Binding Sites, Xenon, Protein Conformation, Crystallography, X-Ray, Structure-Activity Relationship, Hydrogenase, Computer Simulation, Desulfovibrio, Gases, Hydrogen
Models, Molecular, Binding Sites, Xenon, Protein Conformation, Crystallography, X-Ray, Structure-Activity Relationship, Hydrogenase, Computer Simulation, Desulfovibrio, Gases, Hydrogen
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