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PMID: 3015891 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Electron-paramagnetic-resonance spectroscopy of Bacillus subtilis cytochrome b558 in Escherichia coli membranes and in succinate dehydrogenase complex from Bacillus subtilis membranes.

Journal of bacteriology ·Vol. 167 ·No. 2 ·1986-08-00 ·Pages 735-9

Hederstedt L, Andersson KK

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.

MeSH Terms
Bacillus subtilis Cell Membrane/enzymology,ultrastructure Cytochrome b Group Electron Spin Resonance Spectroscopy Escherichia coli Heme NADPH Oxidases Succinate Dehydrogenase
Chemicals
Cytochrome b Group Heme cytochrome b558 Succinate Dehydrogenase NADPH Oxidases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hederstedt L
Andersson K K
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30 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1986-08-00
Pages
735-9
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC212955
Subset
IM
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