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

Dong, Geng LU ; Phung, Quan Manh; Hallaert, Simon D.; Pierloot, Kristine and Ryde, Ulf LU (2017) In Physical Chemistry Chemical Physics 19(16). p.10590-10601
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... (More)

[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.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Physical Chemistry Chemical Physics
volume
19
issue
16
pages
12 pages
publisher
The Royal Society of Chemistry
external identifiers
  • scopus:85020003351
  • wos:000400117700042
ISSN
1463-9076
DOI
10.1039/c7cp01331k
language
English
LU publication?
yes
id
08ffb7f9-8ac0-449f-b5ab-777fb10c2240
date added to LUP
2017-06-30 09:22:09
date last changed
2017-09-18 11:37:04
@article{08ffb7f9-8ac0-449f-b5ab-777fb10c2240,
  abstract     = {<p>[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<sub>2</sub> as a clean fuel. In this paper, we have studied how H<sub>2</sub> 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<sub>2</sub> binding to Ni in the singlet state is the most favourable by at least 47 kJ mol<sup>-1</sup>. In addition, the TPSS functional gives more accurate energies than B3LYP for this system.</p>},
  author       = {Dong, Geng and Phung, Quan Manh and Hallaert, Simon D. and Pierloot, Kristine and Ryde, Ulf},
  issn         = {1463-9076},
  language     = {eng},
  number       = {16},
  pages        = {10590--10601},
  publisher    = {The Royal Society of Chemistry},
  series       = {Physical Chemistry Chemical Physics},
  title        = {H<sub>2</sub> binding to the active site of [NiFe] hydrogenase studied by multiconfigurational and coupled-cluster methods},
  url          = {http://dx.doi.org/10.1039/c7cp01331k},
  volume       = {19},
  year         = {2017},
}