Jump to main content
Jump to site search

Issue 16, 2017
Previous Article Next Article

H2 binding to the active site of [NiFe] hydrogenase studied by multiconfigurational and coupled-cluster methods

Author affiliations

Abstract

[NiFe] hydrogenases catalyse the reversible conversion of molecular hydrogen to protons and electrons. This seemingly simple reaction has attracted much attention because of the prospective use of H2 as a clean fuel. In this paper, we have studied how H2 binds to the active site of this enzyme. Combined quantum mechanical and molecular mechanics (QM/MM) optimisation was performed to obtain the geometries, using both the TPSS and B3LYP density-functional theory (DFT) methods and considering both the singlet and triplet states of the Ni(II) ion. To get more accurate energies and obtain a detailed account of the surroundings, we performed calculations with 819 atoms in the QM region. Moreover, coupled-cluster calculations with singles, doubles, and perturbatively treated triples (CCSD(T)) and cumulant-approximated second-order perturbation theory based on the density-matrix renormalisation group (DMRG-CASPT2) were carried out using three models to decide which DFT methods give the most accurate structures and energies. Our calculations show that H2 binding to Ni in the singlet state is the most favourable by at least 47 kJ mol−1. In addition, the TPSS functional gives more accurate energies than B3LYP for this system.

Graphical abstract: H2 binding to the active site of [NiFe] hydrogenase studied by multiconfigurational and coupled-cluster methods

Back to tab navigation

Supplementary files

Publication details

The article was received on 01 Mar 2017, accepted on 30 Mar 2017 and first published on 31 Mar 2017


Article type: Paper
DOI: 10.1039/C7CP01331K
Citation: Phys. Chem. Chem. Phys., 2017,19, 10590-10601
  • Open access: Creative Commons BY license
  •   Request permissions

    H2 binding to the active site of [NiFe] hydrogenase studied by multiconfigurational and coupled-cluster methods

    G. Dong, Q. M. Phung, S. D. Hallaert, K. Pierloot and U. Ryde, Phys. Chem. Chem. Phys., 2017, 19, 10590
    DOI: 10.1039/C7CP01331K

    This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author

Spotlight

Advertisements