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

Author

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  • Yasuhito Shomura

    (Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun
    RIKEN SPring-8 Center, 1-1-1 Koto, Sayo-gun, Sayo-cho)

  • Ki-Seok Yoon

    (College of Agriculture, Ibaraki University, 3-21-1 Chu-ou, Ami-machi, Inashiki-gun
    Present address: Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan.)

  • 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
    RIKEN SPring-8 Center, 1-1-1 Koto, Sayo-gun, Sayo-cho
    Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST), Kawaguchi Center Building, 4-1-8 Honcho, Kawaguchi-shi)

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.

Suggested Citation

  • Yasuhito Shomura & Ki-Seok Yoon & Hirofumi Nishihara & Yoshiki Higuchi, 2011. "Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase," Nature, Nature, vol. 479(7372), pages 253-256, November.
    • Handle: RePEc:nat:nature:v:479:y:2011:i:7372:d:10.1038_nature10504
    DOI: 10.1038/nature10504
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