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Main Title: Insights into the structure of the active site of the O-2-tolerant membrane bound [NiFe] hydrogenase of R. eutropha H16 by molecular modelling
Author(s): Rippers, Yvonne
Utesch, Tillmann
Hildebrandt, Peter
Zebger, Ingo
Mroginski, Maria Andrea
Type: Article
Language Code: en
Abstract: Structural models for the Ni-B state of the wild-type and C81S protein variant of the membrane-bound [NiFe] hydrogenase from Ralstonia eutrophaH16 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.
Issue Date: 2011
Date Available: 1-Jul-2016
DDC Class: 540 Chemie und zugeordnete Wissenschaften
Sponsor/Funder: DFG, EXC 314, Unifying Concepts in Catalysis
Journal Title: Physical chemistry, chemical physics
Publisher: Royal Society of Chemistry
Publisher Place: Cambridge
Volume: 13
Issue: 36
Publisher DOI: 10.1039/c1cp21045a
Page Start: 16146
Page End: 16149
EISSN: 1463-9084
ISSN: 1463-9076
Notes: Dieser Beitrag ist mit Zustimmung des Rechteinhabers aufgrund einer (DFG geförderten) Allianz- bzw. Nationallizenz frei zugänglich.
This publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively.
Appears in Collections:Inst. Chemie » Publications

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