Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 19, Issue 16, Pages 10590-10601Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7cp01331k
Keywords
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Funding
- Swedish research council [2014-5540]
- Flemish Science Foundation (FWO) [G.0863.13]
- China Scholarship Council [201406360045]
- COST through Action [CM1305]
- Hercules Foundation
- Flemish Government-department EWI
- [COST-STSM-CM1305-30814]
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[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 H-2 as a clean fuel. In this paper, we have studied how H-2 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 H-2 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.
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