Redox tuning of the H-cluster by second coordination sphere amino acids in the sensory [FeFe] hydrogenase from <i>Thermotoga maritima</i>-Reference-Cited by-同舟云学术

Redox tuning of the H-cluster by second coordination sphere amino acids in the sensory [FeFe] hydrogenase from Thermotoga maritima

Published:2023 Issue:13 Volume:14 Page:3682-3692
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Chongdar Nipa¹²^ORCID,Rodríguez-Maciá Patricia¹³^ORCID,Reijerse Edward J.¹^ORCID,Lubitz Wolfgang¹^ORCID,Ogata Hideaki⁴^ORCID,Birrell James A.¹⁵^ORCID

Affiliation:

1. Max Planck Institute for Chemical Energy Conversion, Stiftstraße 34-36, 45470 Mülheim an der Ruhr, Germany

2. CSIR-National Institute of Oceanography, Dona Paula-403004, Goa, India

3. Department of Chemistry, Inorganic Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QR, UK

4. Graduate School of Life Science, University of Hyogo, Koto 3-2-1, Kamigori, Ako, 678-1297 Hyogo, Japan

5. School of Life Sciences, University of Essex, Colchester, CO4 3SQ, UK

Abstract

Site-directed mutagenesis of the sensory [FeFe] hydrogenase from Thermotoga maritima reveals new insight into how the protein environment tunes the active site properties for its sensory role.

Funder

Linacre College, University of Oxford

Max-Planck-Gesellschaft

Japan Society for the Promotion of Science

Deutsche Forschungsgemeinschaft

University of Oxford

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2023/SC/D2SC06432D

Reference41 articles.

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4. Genomic and metagenomic surveys of hydrogenase distribution indicate H2 is a widely utilised energy source for microbial growth and survival

5. The catalytic cycle of [FeFe] hydrogenase: A tale of two sites

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