H2binding to the active site of [NiFe] hydrogenase studied by multiconfigurational and coupled-cluster methods-Reference-Cited by-同舟云学术

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H2binding to the active site of [NiFe] hydrogenase studied by multiconfigurational and coupled-cluster methods

Published:2017 Issue:16 Volume:19 Page:10590-10601
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Dong Geng¹²³⁴,Phung Quan Manh⁵⁶⁷⁸,Hallaert Simon D.⁵⁶⁷⁸,Pierloot Kristine⁵⁶⁷⁸^ORCID,Ryde Ulf¹²³⁴^ORCID

Affiliation:

1. Department of Theoretical Chemistry

2. Lund University

3. SE-221 00 Lund

4. Sweden

5. Department of Chemistry

6. University of Leuven

7. B-3001 Leuven

8. Belgium

Abstract

CCSD(T) and DMRG-CASPT2 calculations show that H₂prefers to bind to Ni rather than to Fe in [NiFe] hydrogenase.

Funder

Vetenskapsrådet

Fonds Wetenschappelijk Onderzoek

China Scholarship Council

European Cooperation in Science and Technology

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2017/CP/C7CP01331K

Reference74 articles.

1. Hydrogenases

2. Removal of the bridging ligand atom at the Ni–Fe active site of [NiFe] hydrogenase upon reduction with H2, as revealed by X-ray structure analysis at 1.4 Å resolution

3. Activation and Inactivation of Hydrogenase Function and the Catalytic Cycle: Spectroelectrochemical Studies

4. [NiFe] and [FeFe] Hydrogenases Studied by Advanced Magnetic Resonance Techniques

5. Investigating and Exploiting the Electrocatalytic Properties of Hydrogenases

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4. Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase;Chemical Reviews;2022-07-18

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