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多巴胺β-单加氧酶的酶结合铜。添加铜对全酶的激活作用以及水杨酸铜使电子传递与羟基化解偶联。

Enzyme-bound copper of dopamine beta-monooxygenase. Activation of the holoenzyme by added copper and uncoupling of electron transfer from hydroxylation by copper salicylate.

作者信息

Skotland T, Ljones T

出版信息

J Inorg Biochem. 1983 Feb;18(1):11-8. doi: 10.1016/0162-0134(83)85035-1.

DOI:10.1016/0162-0134(83)85035-1
PMID:6834029
Abstract

preparations of dopamine beta-monooxygenase containing a full complement of copper (4.2 copper atoms per tetramer) show increased ascorbate-supported catalytic activities after addition of an excess of copper ions. The significance of this observation on the question of the number of copper atoms per active site is discussed. Low molecular weight copper complexes such as copper salicylate cause uncoupling of electron transport from hydroxylation. This uncoupling is probably the reason for the well-known inhibition of this enzyme observed at high copper concentration. The onset of inhibition by the copper chelator bathocuproine disulfonate occurs on a faster time scale than the removal of enzyme-bound copper. Nevertheless, the copper removal is sufficiently rapid to require that it be considered in interpretation of inhibition experiments with chelators.

摘要

含有完整铜补充量(每个四聚体有4.2个铜原子)的多巴胺β-单加氧酶制剂在添加过量铜离子后,抗坏血酸支持的催化活性增加。讨论了这一观察结果对每个活性位点铜原子数量问题的意义。低分子量铜络合物如水杨酸铜会导致电子传递与羟基化解偶联。这种解偶联可能是在高铜浓度下观察到的该酶众所周知的抑制作用的原因。铜螯合剂bathocuproine disulfonate的抑制作用开始的时间尺度比酶结合铜的去除更快。然而,铜的去除足够快,以至于在解释螯合剂抑制实验时需要考虑这一点。

相似文献

1
Enzyme-bound copper of dopamine beta-monooxygenase. Activation of the holoenzyme by added copper and uncoupling of electron transfer from hydroxylation by copper salicylate.多巴胺β-单加氧酶的酶结合铜。添加铜对全酶的激活作用以及水杨酸铜使电子传递与羟基化解偶联。
J Inorg Biochem. 1983 Feb;18(1):11-8. doi: 10.1016/0162-0134(83)85035-1.
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[Purification of dopamine-beta-monooxygenase and extremely acidic, copper-containing proteins from the adrenal medulla. Extremely acidic, copper-containing proteins as electron donors for dopamine-beta-monooxygenase].
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The enzyme-bound copper of dopamine beta-monooxygenase. Reaction with copper chelators, preparation of the apoprotein, and kinetics of the reconstitution by added copper.
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引用本文的文献

1
Kinetic and e.p.r. studies of cyanide and azide binding to the copper sites of dopamine (3,4-dihydroxyphenethylamine) beta-mono-oxygenase.氰化物和叠氮化物与多巴胺(3,4-二羟基苯乙胺)β-单加氧酶铜位点结合的动力学和电子顺磁共振研究。
Biochem J. 1984 Jun 1;220(2):447-54. doi: 10.1042/bj2200447.