大肠杆菌膜中枯草芽孢杆菌细胞色素b558以及枯草芽孢杆菌膜中琥珀酸脱氢酶复合物的电子顺磁共振光谱分析
Electron-paramagnetic-resonance spectroscopy of Bacillus subtilis cytochrome b558 in Escherichia coli membranes and in succinate dehydrogenase complex from Bacillus subtilis membranes.
作者信息
Hederstedt L, Andersson K K
出版信息
J Bacteriol. 1986 Aug;167(2):735-9. doi: 10.1128/jb.167.2.735-739.1986.
Abstract
Cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex was studied by electron-paramagnetic-resonance (EPR) spectroscopy. The cytochrome amplified in Escherichia coli membranes by expression of the cloned cytochrome gene and in the succinate dehydrogenase complex immunoprecipitated from solubilized B. subtilis membranes, respectively, is shown to be low spin with a highly anisotropic (gmax approximately equal to 3.5) EPR signal. The amino acid residues most likely forming fifth and sixth axial ligands to heme in cytochrome b558 are discussed on the basis of the EPR signal and the recently determined gene sequence (K. Magnusson, M. Philips, J.R. Guest, and L. Rutberg, J. Bacteriol. 166:1067-1071, 1986) and in comparison with other b-type cytochromes.
摘要
利用电子顺磁共振（EPR）光谱对枯草芽孢杆菌琥珀酸脱氢酶复合物的细胞色素b558进行了研究。分别通过克隆的细胞色素基因在大肠杆菌膜中表达以及从溶解的枯草芽孢杆菌膜中免疫沉淀的琥珀酸脱氢酶复合物中扩增得到的细胞色素，显示为低自旋，具有高度各向异性（gmax约等于3.5）的EPR信号。基于EPR信号、最近确定的基因序列（K. Magnusson、M. Philips、J.R. Guest和L. Rutberg，《细菌学杂志》166:1067 - 1071，1986）并与其他b型细胞色素进行比较，讨论了最有可能形成细胞色素b558中血红素第五和第六轴向配体的氨基酸残基。
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Cytochrome b reducible by succinate in an isolated succinate dehydrogenase-cytochrome b complex from Bacillus subtilis membranes.在来自枯草芽孢杆菌膜的分离的琥珀酸脱氢酶 - 细胞色素b复合物中可被琥珀酸还原的细胞色素b。
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