Structural basis of [NiFe] hydrogenase maturation by Hyp proteins
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Satoshi Watanabe
Satoshi Watanabe obtained his PhD in chemistry from Kyoto University, Japan in 2007. His PhD work was focused on the molecular mechanism of an oxidative stress sensor protein SoxR by X-ray crystallography. He has been working as a postdoctoral fellow in Prof. Kunio Miki’s laboratory at Kyoto University. Current research focuses on the structural and functional studies of the assembly of complex biological metallocenters.
Daisuke Sasaki was born in Gifu, Japan in 1984. He studied structural biology and X-ray crystallography in Prof. Kunio Miki’s laboratory at Graduate School of Science, Kyoto University, Japan. After received his PhD from Kyoto University, he moved to Prof. Motomu Kanai’s group at Graduate School of Pharmaceutical Science, The University of Tokyo, Japan and is now working as a postdoctoral fellow. His current research focus is on structure-based drug design and chemical synthesis.
Taiga Tominaga graduated in chemistry from Kyoto University, Japan in 2008. He is a PhD student of Graduate School of Science, Kyoto University. He studies structural biology and X-ray crystallography in Prof. Kunio Miki’s laboratory. His research currently focuses on [NiFe] hydrogenase maturation proteins; Hyp proteins.
Kunio Miki obtained his PhD in chemistry from Osaka University, Japan in 1981. Since 1978, he worked as Research Associate in Faculty of Engineering, Osaka University. He joined Prof. Robert Huber’s laboratory in Max-Planck-Institut für Biochemie, Martinsried, Germany as a visiting scientific fellow in 1982–1983. He moved to Tokyo Institute of Technology, Japan as Associate Professor in 1991. Since 1994, he is Full Professor of Department of Chemistry, Graduate School of Science, Kyoto University, Japan, and his laboratory is focused on works of protein crystallography and structural biology.
Abstract
[NiFe] hydrogenases catalyze reversible hydrogen production/consumption. The active site of [NiFe] hydrogenases contains a complex NiFe(CN)2CO center, and the biosynthesis/maturation of these enzymes is a complex and dynamic process, primarily involving six Hyp proteins (HypABCDEF). HypA and HypB are involved in the Ni insertion, whereas the other four Hyp proteins (HypCDEF) are required for the biosynthesis, assembly and insertion of the Fe(CN)2CO group. Over the last decades, a large number of functional and structural studies on maturation proteins have been performed, revealing detailed functions of each Hyp protein and the framework of the maturation pathway. This article will focus on recent advances in structural studies of the Hyp proteins and on mechanistic insights into the [NiFe] hydrogenase maturation.
About the authors
Satoshi Watanabe obtained his PhD in chemistry from Kyoto University, Japan in 2007. His PhD work was focused on the molecular mechanism of an oxidative stress sensor protein SoxR by X-ray crystallography. He has been working as a postdoctoral fellow in Prof. Kunio Miki’s laboratory at Kyoto University. Current research focuses on the structural and functional studies of the assembly of complex biological metallocenters.
Daisuke Sasaki was born in Gifu, Japan in 1984. He studied structural biology and X-ray crystallography in Prof. Kunio Miki’s laboratory at Graduate School of Science, Kyoto University, Japan. After received his PhD from Kyoto University, he moved to Prof. Motomu Kanai’s group at Graduate School of Pharmaceutical Science, The University of Tokyo, Japan and is now working as a postdoctoral fellow. His current research focus is on structure-based drug design and chemical synthesis.
Taiga Tominaga graduated in chemistry from Kyoto University, Japan in 2008. He is a PhD student of Graduate School of Science, Kyoto University. He studies structural biology and X-ray crystallography in Prof. Kunio Miki’s laboratory. His research currently focuses on [NiFe] hydrogenase maturation proteins; Hyp proteins.
Kunio Miki obtained his PhD in chemistry from Osaka University, Japan in 1981. Since 1978, he worked as Research Associate in Faculty of Engineering, Osaka University. He joined Prof. Robert Huber’s laboratory in Max-Planck-Institut für Biochemie, Martinsried, Germany as a visiting scientific fellow in 1982–1983. He moved to Tokyo Institute of Technology, Japan as Associate Professor in 1991. Since 1994, he is Full Professor of Department of Chemistry, Graduate School of Science, Kyoto University, Japan, and his laboratory is focused on works of protein crystallography and structural biology.
©2012 by Walter de Gruyter Berlin Boston
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Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- No end in sight: the development of protein crystallography in Martinsried
- Highlight: No End in Sight: The Development of Protein Crystallography in Martinsried
- Functional and structural insights into astacin metallopeptidases
- β-Trefoil inhibitors – from the work of Kunitz onward
- Structural basis of the TAL effector–DNA interaction
- Nature’s way of handling a greenhouse gas: the copper-sulfur cluster of purple nitrous oxide reductase
- Rustless translation
- Structural basis of [NiFe] hydrogenase maturation by Hyp proteins
- Covalent and non-covalent reversible proteasome inhibition
- Structural origins of AGC protein kinase inhibitor selectivities: PKA as a drug discovery tool
- Structural analysis of the C-terminal domain of the spliceosomal helicase Prp22
- N-terminal acetylation of annexin A2 is required for S100A10 binding
- Withaferin A binds covalently to the N-terminal domain of annexin A2
- PhoB transcriptional activator binds hierarchically to pho box promoters
- Research Articles/Short Communications
- Protein Structure and Function
- Biochemical and functional characterization of human phospholipid scramblase 4 (hPLSCR4)
- Cell Biology and Signaling
- Dual-specificity phosphatases are targets of the Wnt/β-catenin pathway and candidate mediators of β-catenin/Ras signaling interactions
- Proteolysis
- Inhibition of Aeromonas sobria serine protease (ASP) by α2-macroglobulin
