枯草芽孢杆菌caa3型氧化酶的铜结合位点是一个混合价态的双核铜中心。

The CuAsite of the caa3-type oxidase of Bacillus subtilis is a mixed-valence binuclear copper centre.

作者信息

von Wachenfeldt C, de Vries S, van der Oost J

机构信息

Department of Molecular and Cellular Biology, BioCentrum Amsterdam, Vrije Universiteit, The Netherlands.

出版信息

FEBS Lett. 1994 Feb 28;340(1-2):109-13. doi: 10.1016/0014-5793(94)80182-7.

DOI:10.1016/0014-5793(94)80182-7

PMID:8119391

Abstract

A copper-containing domain of the caa3-type oxidase from Bacillus subtilis has been expressed as a water-soluble protein in the cytoplasm of Escherichia coli. Electron paramagnetic resonance (EPR) spectra of this purple domain show well-resolved lines in the gz resonance, both at X-band and S-band frequencies. Interpretation of EPR spectra and analytical data indicate a binuclear copper site consisting of one Cu2+ and one Cu1+. This copper site closely resembles CuA in subunit II of cytochrome c oxidase and is shown here to be a mixed-valence [Cu2+-Cu1+] binuclear centre.

摘要

来自枯草芽孢杆菌的caa3型氧化酶的含铜结构域已作为一种水溶性蛋白在大肠杆菌细胞质中表达。该紫色结构域的电子顺磁共振（EPR）光谱在X波段和S波段频率下的gz共振中都显示出分辨率良好的谱线。EPR光谱和分析数据的解释表明存在一个由一个Cu2+和一个Cu1+组成的双核铜位点。这个铜位点与细胞色素c氧化酶亚基II中的CuA非常相似，并且在此处显示为一个混合价态的[Cu2+-Cu1+]双核中心。