Satoshi Watanabe, Daisuke Sasaki, Taiga Tominaga, Kunio Miki
Department of Chemistry, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.
Biological chemistry 2012 OctNiFe] 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.
Satoshi Watanabe, Daisuke Sasaki, Taiga Tominaga, Kunio Miki. Structural basis of [NiFe] hydrogenase maturation by Hyp proteins. Biological chemistry. 2012 Oct;393(10):1089-100
PMID: 23096350
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