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Reviews in Inorganic Chemistry

Editor-in-Chief: Schulz, Axel

Editorial Board: Aldridge, Simon / Burford, Neil / Cronin, Leroy / Dunbar, Kim / Holthausen, Max / Huppertz, Hubert / Liu, Xiaoming / Rosenthal, Uwe / Schiller, Alexander / Schulz, Stephan / Senker, Jürgen / Hänisch, Carsten / Yoon, Kyung / Zhang, Xian-Ming


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Volume 33, Issue 4

Issues

Structural aspects of [NiFe]-hydrogenases

Yasuhito Shomura
  • Corresponding author
  • Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan
  • RIKEN SPring-8 Center, 1-1-1 Koto, Sayo-gun, Sayo-cho, Hyogo 679-5148, Japan
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Yoshiki Higuchi
  • Corresponding author
  • Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan
  • RIKEN SPring-8 Center, 1-1-1 Koto, Sayo-gun, Sayo-cho, Hyogo 679-5148, Japan
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2013-09-07 | DOI: https://doi.org/10.1515/revic-2013-0005

Abstract

Enzymes that naturally contain an organometallic complex are highly rare. Hydrogenases commonly include iron carbonyl(s) at the active site and play central roles in the hydrogen metabolism of microorganisms. [NiFe]-hydrogenases that harbor an Ni-Fe(CN)2CO complex at the active site most widely exist among organisms, compared with the other two types, [FeFe]- and [Fe]-hydrogenases. Since the first crystal structure report in 1995, structural information of the Ni-Fe cluster with various redox/substrate-bound states has been obtained, although details of the reaction mechanisms are poorly understood. While the subunit composition, physiological function, and spectroscopic/biochemical properties of [NiFe]-hydrogenases are diverse, structural information of only a limited group of the enzymes is available so far. In this paper, structural aspects of [NiFe]-hydrogenases are reviewed and recent progresses in understanding the mechanism of an O2-tolerant property of limited members and active site assembling of [NiFe]-hydrogenases are described.

Keywords: crystal structure; enzyme; hydrogen; iron; nickel

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About the article

Yasuhito Shomura

Yasuhito Shomura graduated from Shizuoka University, Japan (1998), and obtained his PhD from Kyoto University, Japan (2003) under the supervision of Prof. Kunio Miki. After a postdoctoral stay at Prof. F. Ulrich Hartl’s laboratory of Max-Planck-Institute für Biochemie (2003–2005), he has joined Prof. Yoshiki Higuchi’s laboratory as an assistant professor. In 2013, he was awarded a Minister of Education, Culture, Sports Science and Technology of Japan for young scientist award. His research activities include the structure and reaction/assembling mechanism of hydrogenases and other various proteins.

Yoshiki Higuchi

Yoshiki Higuchi studied chemistry from 1975 to 1979 at Osaka University, Japan, and did his PhD thesis in 1984 under the supervision of Prof. Masao Kakudo at Institute for Protein Research, Osaka University. He was appointed as an Assistant Professor of Himeji Institute of Technology in 1985, moved to Kyoto University in 1995 as an Associate Professor of Graduate School of Science. He moved to Himeji Institute of Technology, as a Professor of the Graduate School of Science in 2002, and is currently a Professor of the Graduate School of Life Science, University of Hyogo. He received the Award of the Crystallographic Society of Japan in 1999. At present, he is involved in structural chemistry on hydrogenases including those from other sources, as well as on protein-protein interactions in the cells of higher organisms.


Corresponding authors: Yasuhito Shomura and Yoshiki Higuchi, Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan; and RIKEN SPring-8 Center, 1-1-1 Koto, Sayo-gun, Sayo-cho, Hyogo 679-5148, Japan, e-mail: ,


Received: 2013-03-29

Accepted: 2013-08-05

Published Online: 2013-09-07

Published in Print: 2013-12-01


Citation Information: Reviews in Inorganic Chemistry, Volume 33, Issue 4, Pages 173–192, ISSN (Online) 2191-0227, ISSN (Print) 0193-4929, DOI: https://doi.org/10.1515/revic-2013-0005.

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