title: Insights into the structure of the active site of the O2-tolerant membrane bound [NiFe] hydrogenase of R. eutropha H16 by molecular modelling.
abstract: Structural models for the Ni-B state of the wild-type and C81S protein variant of the membrane-bound [NiFe] hydrogenase from Ralstonia eutropha H16 were derived by applying the homology model technique combined with molecular simulations and a hybrid quantum mechanical/molecular mechanical approach. The active site structure was assessed by comparing calculated and experimental IR spectra, confirming the view that the active site structure is very similar to those of anaerobic standard hydrogenases. In addition, the data suggest the presence of a water molecule in the second coordination sphere of the active centre.
authors.affiliation: Institut f. Chemie, Sekr. PC14, Technische Universität Berlin, Straße des 17, Juni 135, D-10623 Berlin, Germany.
authors.forename: Yvonne
authors.initials: Y
authors.lastname: Rippers
authors.forename: Tillmann
authors.initials: T
authors.lastname: Utesch
authors.forename: Peter
authors.initials: P
authors.lastname: Hildebrandt
authors.forename: Ingo
authors.initials: I
authors.lastname: Zebger
authors.forename: Maria Andrea
authors.initials: MA
authors.lastname: Mroginski
mesh_terms: D020134:Catalytic Domain; D020118:Cupriavidus necator / Q000201:enzymology*; D006864:Hydrogenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D009154:Mutation; D010100:Oxygen / Q000737:chemistry; D011485:Protein Binding; D011789:Quantum Theory; D013055:Spectrophotometry, Infrared
chemical_list: C043296:nickel-iron hydrogenase; D006864:Hydrogenase; D010100:Oxygen