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

Hederstedt, Lars LU and Andersson, K Kristoffer (1986) In Journal of Bacteriology 167(2). p.735-739
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... (More)
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. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Bacteriology
volume
167
issue
2
pages
735 - 739
publisher
American Society for Microbiology
ISSN
0021-9193
DOI
10.1128/jb.167.2.735-739.1986
language
English
LU publication?
no
id
39eb68c4-ef4a-4e18-8a89-b23ba8eb9947
date added to LUP
2017-07-18 11:06:59
date last changed
2017-11-16 14:57:56
@article{39eb68c4-ef4a-4e18-8a89-b23ba8eb9947,
  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. },
  author       = {Hederstedt, Lars and Andersson, K Kristoffer},
  issn         = {0021-9193},
  language     = {eng},
  number       = {2},
  pages        = {735--739},
  publisher    = {American Society for Microbiology},
  series       = {Journal of Bacteriology},
  title        = {Electron-paramagnetic-resonance spectroscopy of <em>Bacillus subtilis</em> cytochrome b558 in <em>Escherichia coli</em> membranes and in succinate dehydrogenase complex from <em>Bacillus subtilis</em> membranes},
  url          = {http://dx.doi.org/10.1128/jb.167.2.735-739.1986},
  volume       = {167},
  year         = {1986},
}