硒代半胱氨酸
化学
甲酸脱氢酶
格式化
辅因子
钼辅因子
钼
立体化学
活动站点
结晶学
电子转移
催化作用
无机化学
光化学
生物化学
酶
半胱氨酸
作者
Jeffrey C. Boyington,Vadim N. Gladyshev,Sergei V. Khangulov,Thressa C. Stadtman,Peter D. Sun
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:1997-02-28
卷期号:275 (5304): 1305-1308
被引量:544
标识
DOI:10.1126/science.275.5304.1305
摘要
Formate dehydrogenase H from Escherichia coli contains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and an Fe 4 S 4 cluster at the active site and catalyzes the two-electron oxidation of formate to carbon dioxide. The crystal structures of the oxidized [Mo(VI), Fe 4 S 4(ox) ] form of formate dehydrogenase H (with and without bound inhibitor) and the reduced [Mo(IV), Fe 4 S 4(red) ] form have been determined, revealing a four-domain αβ structure with the molybdenum directly coordinated to selenium and both MGD cofactors. These structures suggest a reaction mechanism that directly involves SeCys 140 and His 141 in proton abstraction and the molybdenum, molybdopterin, Lys 44 , and the Fe 4 S 4 cluster in electron transfer.
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