Electron-paramagnetic-resonance spectroscopy of Bacillus subtilis cytochrome b558 in Escherichia coli membranes and in succinate dehydrogenase complex from Bacillus subtilis membranes.
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.
D001412:Bacillus subtilis; D002462:Cell Membrane / Q000201:enzymology / Q000648:ultrastructure; D003573:Cytochrome b Group; D004578:Electron Spin Resonance Spectroscopy; D004926:Escherichia coli; D006418:Heme; D019255:NADPH Oxidases; D013385:Succinate Dehydrogenase
D003573:Cytochrome b Group; D006418:Heme; C036888:cytochrome b558; D013385:Succinate Dehydrogenase; D019255:NADPH Oxidases