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本文引用的文献

1
Hydroxylamine reductase activity of the hybrid cluster protein from Escherichia coli.大肠杆菌杂交簇蛋白的羟胺还原酶活性
J Bacteriol. 2002 Nov;184(21):5898-902. doi: 10.1128/JB.184.21.5898-5902.2002.
2
Carbon monoxide dehydrogenase from Rhodospirillum rubrum produces formate.来自红螺菌的一氧化碳脱氢酶可产生甲酸。
J Biol Inorg Chem. 2002 Sep;7(7-8):810-4. doi: 10.1007/s00775-002-0365-z. Epub 2002 Apr 30.
3
The Ni-containing carbon monoxide dehydrogenase family: light at the end of the tunnel?含镍一氧化碳脱氢酶家族：曙光在前？
Biochemistry. 2002 Feb 19;41(7):2097-105. doi: 10.1021/bi015932+.
4
Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase.一氧化碳上的生命：深红红螺菌镍铁硫一氧化碳脱氢酶的X射线结构
Proc Natl Acad Sci U S A. 2001 Oct 9;98(21):11973-8. doi: 10.1073/pnas.211429998. Epub 2001 Oct 2.
5
Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster.一氧化碳脱氢酶的晶体结构揭示了一个[Ni-4Fe-5S]簇。
Science. 2001 Aug 17;293(5533):1281-5. doi: 10.1126/science.1061500.
6
Redox-dependent activation of CO dehydrogenase from Rhodospirillum rubrum.来自红螺菌的一氧化碳脱氢酶的氧化还原依赖性激活
Proc Natl Acad Sci U S A. 2001 Jul 3;98(14):7690-3. doi: 10.1073/pnas.141230698. Epub 2001 Jun 19.
7
Hybrid-cluster protein (HCP) from Desulfovibrio vulgaris (Hildenborough) at 1.6 A resolution.来自普通脱硫弧菌（希登伯勒菌株）的混合簇蛋白（HCP），分辨率为1.6埃。
Biochemistry. 2000 Dec 12;39(49):15044-54. doi: 10.1021/bi001483m.
8
Evidence for a ligand CO that is required for catalytic activity of CO dehydrogenase from Rhodospirillum rubrum.来自红螺菌的一氧化碳脱氢酶催化活性所需的配体一氧化碳的证据。
Biochemistry. 2000 Jul 11;39(27):7956-63. doi: 10.1021/bi992958g.
9
Substitution of valine for histidine 265 in carbon monoxide dehydrogenase from Rhodospirillum rubrum affects activity and spectroscopic states.在红螺菌一氧化碳脱氢酶中，用缬氨酸替代组氨酸265会影响其活性和光谱状态。
J Biol Chem. 1998 Feb 13;273(7):4059-64. doi: 10.1074/jbc.273.7.4059.
10
Unleashing hydrogenase activity in carbon monoxide dehydrogenase/acetyl-CoA synthase and pyruvate:ferredoxin oxidoreductase.释放一氧化碳脱氢酶/乙酰辅酶A合成酶和丙酮酸：铁氧化还原蛋白氧化还原酶中的氢化酶活性。
Biochemistry. 1996 Dec 10;35(49):15814-21. doi: 10.1021/bi9615598.

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.

DOI:10.1128/JB.184.21.5894-5897.2002
PMID:12374822
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC135374/
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。