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首页> 外文期刊>Angewandte Chemie >A Nickel-Alkyl Bond in an Inactivated State of the Enzyme Catalyzing Methane Formation
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A Nickel-Alkyl Bond in an Inactivated State of the Enzyme Catalyzing Methane Formation

机译:酶催化甲烷形成的失活状态下的镍烷基键

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摘要

The cobalt-carbon bonds of methyl cobalamin and adenosyl cobalamin are the only transition-metal-alkyl bonds verified to date in the active site of enzymes.Methyl-nickel bonds have been postulated to be formed during two enzyme-catalyzed steps,for which,however,experimental evidence has not been provided.These reactions are the synthesis of acetyl-coenzyme A from methyl tetrahydrofolate,carbon monoxide,and coenzyme A when catalyzed by acetyl-coenzyme A synthase(decarbonylase),and methane formation from methyl-coenzyme M and coenzyme B when catalyzed by methyl-coenzyme M reductase(MCR).
机译:甲基钴胺素和腺苷钴胺素的钴-碳键是迄今为止在酶的活性位点唯一被证实的过渡金属-烷基键。据推测,在两个酶催化步骤中会形成甲基-镍键,为此,这些反应是由乙酰辅酶A合酶(脱羰基酶)催化的四氢叶酸甲酯,一氧化碳和辅酶A合成乙酰辅酶A,以及由甲基辅酶M和M形成甲烷。甲基辅酶M还原酶(MCR)催化的辅酶B。

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