大肠杆菌丙酮酸脱氢酶多酶复合体中酶结合硫辛酸流动性的自旋标记研究。
Spin-label study of the mobility of enzyme-bound lipoic acid in the pyruvate dehydrogenase multienzyme complex of Escherichia coli.
作者信息
Ambrose M C, Perham R N
出版信息
Biochem J. 1976 May 1;155(2):429-32. doi: 10.1042/bj1550429.
Abstract
The lipoic acid residues covalently bound to the transacetylase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli were selectively modified by reaction with 4-maleimido-2,2,6,6-tetramethylpiperidino-oxyl. The electron-spin-resonance spectrum of the spin-labelled enzyme indicates that the bound nitroxide groups have high mobilities relative to the protein molecule. This physicochemical evidence is consistent with the view that the dithiolane ring of a lipoyl residue is capable of rapid migration between the active sites of the component enzymes in the catalytic mechanism.
摘要
通过与4-马来酰亚胺基-2,2,6,6-四甲基哌啶氮氧自由基反应，对共价结合于大肠杆菌丙酮酸脱氢酶多酶复合体转乙酰酶组分上的硫辛酸残基进行了选择性修饰。自旋标记酶的电子自旋共振光谱表明，结合的氮氧基团相对于蛋白质分子具有较高的迁移率。这一物理化学证据与硫辛酰残基的二硫杂环戊烷环在催化机制中能够在组分酶的活性位点之间快速迁移的观点一致。
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