甲酸盐脱氢酶的结构与功能关系：研究进展概述。
Structure and function relationship of formate dehydrogenases: an overview of recent progress.
机构信息
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto 606-8502, Japan.
Graduate School of Science, University of Hyogo, Koto 3-2-1 Kamigori, Ako, Hyogo 678-1297, Japan.
出版信息
IUCrJ. 2023 Sep 1;10(Pt 5):544-554. doi: 10.1107/S2052252523006437.
Formate dehydrogenases (FDHs) catalyze the two-electron oxidation of formate to carbon dioxide. FDHs can be divided into several groups depending on their subunit composition and active-site metal ions. Metal-dependent (Mo- or W-containing) FDHs from prokaryotic organisms belong to the superfamily of molybdenum enzymes and are members of the dimethylsulfoxide reductase family. In this short review, recent progress in the structural analysis of FDHs together with their potential biotechnological applications are summarized.
Formate 脱氢酶（FDHs）催化甲酸盐向二氧化碳的两电子氧化。FDHs 可以根据其亚基组成和活性位点金属离子分为几个组。来自原核生物的金属依赖性（含 Mo 或 W）FDHs 属于钼酶超家族，是二甲亚砜还原酶家族的成员。在这篇简短的综述中，总结了 FDHs 的结构分析方面的最新进展及其在生物技术中的潜在应用。
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