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铜蛋白与一氧化氮的反应。

The reactions of copper proteins with nitric oxide.

作者信息

Torres J, Wilson M T

机构信息

Department of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, Essex, UK.

出版信息

Biochim Biophys Acta. 1999 May 5;1411(2-3):310-22. doi: 10.1016/s0005-2728(99)00022-5.

DOI:10.1016/s0005-2728(99)00022-5
PMID:10320665
Abstract

Nitric oxide (NO) can act as a ligand for copper atoms and may also engage in redox chemistry with the metal once bound. Furthermore NO posses an unpaired electron which can couple with the unpaired electron on Cu2+. These properties have been exploited to probe the active sites of copper-containing enzymes and proteins. We review these studies. In addition to the use as a spectroscopic probe for the active site we draw attention to the rapid reactions of NO at the copper sites in Cytochrome c oxidase (CcO) and laccase. These reactions in CcO occur in the ms time range, at low NO concentrations and in the presence of oxygen and may therefore be of physiological relevance to the control of respiration. Finally we speculate on the wider role that NO may play in regulation of an important group of Type 2 copper containing enzymes.

摘要

一氧化氮(NO)可作为铜原子的配体,一旦结合,还可能与金属发生氧化还原反应。此外,NO具有一个未成对电子,该电子可与Cu2+上的未成对电子配对。这些特性已被用于探测含铜酶和蛋白质的活性位点。我们对这些研究进行综述。除了用作活性位点的光谱探针外,我们还关注NO在细胞色素c氧化酶(CcO)和漆酶的铜位点处的快速反应。CcO中的这些反应发生在毫秒时间范围内,在低NO浓度且有氧存在的情况下,因此可能与呼吸控制具有生理相关性。最后,我们推测NO在调控一类重要的含2型铜酶中可能发挥的更广泛作用。

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