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翻訳と辞書　辞書検索 [ 開発暫定版 ] スポンサード リンク Iron-sulfur protein ： ウィキペディア英語版 Iron-sulfur protein Iron-sulfur proteins are proteins characterized by the presence of iron-sulfur clusters containing sulfide-linked di-, tri-, and tetrairon centers in variable oxidation states. Iron-sulfur clusters are found in a variety of metalloproteins, such as the ferredoxins, as well as NADH dehydrogenase, hydrogenases, Coenzyme Q - cytochrome c reductase, Succinate - coenzyme Q reductase and nitrogenase.〔S. J. Lippard, J. M. Berg “Principles of Bioinorganic Chemistry” University Science Books: Mill Valley, CA; 1994. ISBN 0-935702-73-3.〕 Iron-sulfur clusters are best known for their role in the oxidation-reduction reactions of mitochondrial electron transport. Both Complex I and Complex II of oxidative phosphorylation have multiple Fe-S clusters. They have many other functions including catalysis as illustrated by aconitase, generation of radicals as illustrated by SAM-dependent enzymes, and as sulfur donors in the biosynthesis of lipoic acid and biotin. Additionally some Fe-S proteins regulate gene expression. Fe-S proteins are vulnerable to attack by biogenic nitric oxide. In most Fe-S proteins, the terminal ligands on Fe are thiolate, but exceptions exist.〔Bak, D. W.; Elliott, S. J., "Alternative FeS cluster ligands: tuning redox potentials and chemistry", Curr. Opin. Chem. Biol. 2014, 19, 50-58. 〕 The prevalence of these proteins on the metabolic pathways of most organisms leads some scientists to theorize that iron-sulfur compounds had a significant role in the origin of life in the Iron-sulfur world theory. ==Structural motifs== In almost all Fe-S proteins, the Fe centers are tetrahedral and the terminal ligands are thiolato sulfur centers from cysteinyl residues. The sulfide groups are either two- or three-coordinated. Three distinct kinds of Fe-S clusters with these features are most common. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Iron-sulfur protein」の詳細全文を読む スポンサード リンク 翻訳と辞書 : 翻訳のためのインターネットリソース Copyright(C) kotoba.ne.jp 1997-2016. All Rights Reserved.