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Insights into the structure of the active site of the O(2)-tolerant membrane bound [NiFe] hydrogenase of R. eutropha H16 by molecular modelling
Citation key Rippers2011
Author Rippers, Yvonne and Utesch, Tillmann and Hildebrandt, Peter and Zebger, Ingo and Mroginski, Maria Andrea
Pages 16146–16149
Year 2011
Journal Physical Chemistry Chemical Physics
Volume 13
Number 36
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.
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