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

Autor:	Michel Frey, E. Claude Hatchikian, Juan C. Fontecilla-Camps, Martin J. Field, Yaël Montet, Patricia Amara, Anne Volbeda, X. Vernede
Rok vydání:	1997
Předmět:	Models Molecular Hydrogenase Xenon Protein Conformation Diffusion chemistry.chemical_element Crystallography X-Ray Biochemistry Molecular dynamics Structure-Activity Relationship Structural Biology Genetics Computer Simulation Binding Sites integumentary system biology Chemistry Resolution (electron density) Active site Crystallography X-ray crystallography biology.protein Desulfovibrio Gases NiFe hydrogenase circulatory and respiratory physiology Hydrogen
Zdroj:	Nature structural biology. 4(7)
ISSN:	1072-8368
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cb1b935afeb50e24121c8e8f3bde38d https://pubmed.ncbi.nlm.nih.gov/9228943 Zobrazit plný text záznamu Full text from SpringerLink