将镍铁硫一氧化碳脱氢酶转化为氢化酶和羟胺还原酶。
Converting the NiFeS carbon monoxide dehydrogenase to a hydrogenase and a hydroxylamine reductase.
作者信息
Heo Jongyun, Wolfe Marcus T, Staples Christopher R, Ludden Paul W
机构信息
Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599-7260, USA.
出版信息
J Bacteriol. 2002 Nov;184(21):5894-7. doi: 10.1128/JB.184.21.5894-5897.2002.
Abstract
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 Cys(531) exhibits substantial uptake hydrogenase activity, and this activity is enhanced by treatment with CO. CODH with valine substituted for His(265) exhibits hydroxylamine reductase activity. Both Cys(531) and His(265) are ligands to the active-site cluster of CODH. Further, CODH with Fe substituted for Ni at the active site acquires hydroxylamine reductase activity.
摘要
在酶的活性位点将一个氨基酸替换为另一个氨基酸通常会降低或消除酶的活性。然而，在某些情况下，酶的特异性会发生改变。在本研究中，我们报告称，在含NiFeS的一氧化碳脱氢酶（CODH）活性位点改变金属配体可将该酶转化为氢化酶或羟胺还原酶。用丙氨酸取代Cys(531)的CODH表现出显著的吸氢酶活性，并且这种活性通过CO处理而增强。用缬氨酸取代His(265)的CODH表现出羟胺还原酶活性。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取代Ni的CODH获得了羟胺还原酶活性。
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