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首页> 外文期刊>Journal of bacteriology >Converting the NiFeS Carbon Monoxide Dehydrogenase to a Hydrogenase and a Hydroxylamine Reductase
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Converting the NiFeS Carbon Monoxide Dehydrogenase to a Hydrogenase and a Hydroxylamine Reductase

机译：将NiFeS一氧化碳脱氢酶转化为氢化酶和羟胺还原酶

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摘要

Substitution of one amino acid for another at the active site of an enzyme usually diminishes or eliminates the activity of the enzyme. In some cases, however, the specificity of the enzyme is changed. In this study, we report that the changing of a metal ligand at the active site of the NiFeS-containing carbon monoxide dehydrogenase (CODH) converts the enzyme to a hydrogenase or a hydroxylamine reductase. CODH with alanine substituted for Cys531 exhibits substantial uptake hydrogenase activity, and this activity is enhanced by treatment with CO. CODH with valine substituted for His265 exhibits hydroxylamine reductase activity. Both Cys531 and His265 are ligands to the active-site cluster of CODH. Further, CODH with Fe substituted for Ni at the active site acquires hydroxylamine reductase activity.
机译：一种氨基酸在酶的活性位点上被另一种氨基酸取代通常会减少或消除该酶的活性。但是，在某些情况下，酶的特异性会改变。在这项研究中，我们报告说，在含NiFeS的一氧化碳脱氢酶（CODH）的活性位点，金属配体的变化将酶转换为氢化酶或羟胺还原酶。丙氨酸取代Cys 531 的CODH表现出显着的摄取氢化酶活性，而用CO处理可以增强该活性。 Cys 531 和His 265 都是CODH活性位点簇的配体。此外，在活性位点用Fe代替Ni的CODH获得羟胺还原酶活性。

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