Insights into the structure of the active site of the O2-tolerant membrane bound [NiFe] hydrogenase of R. eutrophaH16 by molecular modelling

Yvonne Rippers; Tillmann Utesch; Peter Hildebrandt; Ingo Zebger; Maria Andrea Mroginski

doi:10.1039/C1CP21045A

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Insights into the structure of the active site of the O₂-tolerant membrane bound [NiFe] hydrogenase of R. eutrophaH16 by molecular modelling†

Yvonne Rippers,‡^a Tillmann Utesch,‡^a Peter Hildebrandt,^a Ingo Zebger^a and Maria Andrea Mroginski^a

Author affiliations

^a Institut f. Chemie, Sekr. PC14, Technische Universität Berlin, Straße des 17, Juni 135, D-10623 Berlin, Germany
E-mail: andrea.mroginski@tu-berlin.de
Fax: +49 30 31421122
Tel: +49 30 31426403

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.

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Article information

DOI: https://doi.org/10.1039/C1CP21045A
Article type: Communication
Submitted: 04 Apr 2011
Accepted: 27 Jul 2011
First published: 11 Aug 2011

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Phys. Chem. Chem. Phys., 2011,13, 16146-16149

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Insights into the structure of the active site of the O₂-tolerant membrane bound [NiFe] hydrogenase of R. eutrophaH16 by molecular modelling

Y. Rippers, T. Utesch, P. Hildebrandt, I. Zebger and M. A. Mroginski, Phys. Chem. Chem. Phys., 2011, 13, 16146 DOI: 10.1039/C1CP21045A

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