Redox-dependent conformational changes of a proximal [4Fe–4S] cluster in Hyb-type [NiFe]-hydrogenase to protect the active site from O2-Reference-Cited by-同舟云学术

Redox-dependent conformational changes of a proximal [4Fe–4S] cluster in Hyb-type [NiFe]-hydrogenase to protect the active site from O2

Published:2018 Issue:87 Volume:54 Page:12385-12388
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Noor Noor Dina Muhd¹²³⁴⁵,Matsuura Hiroaki¹²³⁴⁵,Nishikawa Koji¹²³⁴⁵,Tai Hulin⁶⁷⁸⁵⁹^ORCID,Hirota Shun⁶⁷⁸⁵⁹^ORCID,Kim Jaehyun¹²³⁴⁵,Kang Jiyoung¹²³⁴⁵,Tateno Masaru¹²³⁴⁵,Yoon Ki-Seok¹⁰¹¹¹²¹³⁵,Ogo Seiji¹⁰¹¹¹²¹³⁵,Kubota Shintaro¹²³⁴⁵,Shomura Yasuhito⁶⁷⁸⁵¹⁴,Higuchi Yoshiki¹²³⁴⁵^ORCID

Affiliation:

1. Department of Life Science

2. Graduate School of Life Science

3. University of Hyogo

4. Hyogo 678-1297

5. Japan

6. Core Research for Evolutional Science and Technology (CREST)

7. Japan Science and Technology Agency (JST)

8. Saitama 332-0012

9. Division of Materials Science

10. Department of Chemistry and Biochemistry

11. Graduate School of Engineering

12. Kyushu University

13. Fukuoka 819-0395

14. Institute of Quantum Beam Science

Abstract

Citrobacter sp. S-77 [NiFe]-hydrogenase harbors a standard [4Fe–4S] cluster proximal to the Ni–Fe active site.

Funder

ENEOS Hydrogen Trust Fund

Core Research for Evolutional Science and Technology

Japan Society for the Promotion of Science

Mitsubishi Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CC/C8CC06261G

Reference23 articles.

1. Occurrence, Classification, and Biological Function of Hydrogenases: An Overview

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

3. Activation Process of [NiFe] Hydrogenase Elucidated by High-Resolution X-Ray Analyses: Conversion of the Ready to the Unready State

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

5. Unusual ligand structure in Ni–Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis

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