Insights into the structure of the active site of the O-2-tolerant membrane bound [NiFe] hydrogenase of R. eutropha H16 by molecular modelling

Rippers, YvonneUtesch, TillmannHildebrandt, PeterZebger, IngoMroginski, Maria Andrea2016-07-012016-07-0120111463-9076https://depositonce.tu-berlin.de/handle/11303/5754http://dx.doi.org/10.14279/depositonce-5374Dieser 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.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.en540 Chemie und zugeordnete WissenschaftenInsights into the structure of the active site of the O-2-tolerant membrane bound [NiFe] hydrogenase of R. eutropha H16 by molecular modellingArticle1463-908421833416