Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase

Yasuhito Shomura, Ki-Seok Yoon, Hirofumi Nishihara and Yoshiki Higuchi ()
Additional contact information
Yasuhito Shomura: Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun
Ki-Seok Yoon: College of Agriculture, Ibaraki University, 3-21-1 Chu-ou, Ami-machi, Inashiki-gun
Hirofumi Nishihara: College of Agriculture, Ibaraki University, 3-21-1 Chu-ou, Ami-machi, Inashiki-gun
Yoshiki Higuchi: Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun

Nature, 2011, vol. 479, issue 7372, 253-256

Abstract: Oxygen-tolerant hydrogenases Hydrogenases are metalloprotein enzymes that catalyse the reversible oxidation of dihydrogen to protons and electrons, a critical pathway in anaerobic metabolism. This reaction is of particular interest for hydrogen-based applications, in fuel cells for instance, but many applications are hindered by the high oxygen sensitivity that is an intrinsic feature of most hydrogenases. Two groups report the structures of oxygen-tolerant hydrogenases, one from the soil bacterium Ralstonia eutropha and the other from the marine bacterium Hydrogenovibrio marinus. The structures shed light on how redox-sensitive active-site intermediates are protected from destruction. Both enzymes feature a novel iron-sulphur centre at the active site, coordinated by a group of cysteine residues.

Date: 2011
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature10504 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:479:y:2011:i:7372:d:10.1038_nature10504

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature10504

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().