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

@article{Dong2017H2BT,
  title={H2 binding to the active site of [NiFe] hydrogenase studied by multiconfigurational and coupled-cluster methods.},
  author={Geng Dong and Quan Manh Phung and Simon D Hallaert and Kristine Pierloot and Ulf Ryde},
  journal={Physical chemistry chemical physics : PCCP},
  year={2017},
  volume={19 16},
  pages={10590-10601}
}
[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… CONTINUE READING
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