Electron-paramagnetic-resonance spectroscopy of Bacillus subtilis cytochrome b558 in Escherichia coli membranes and in succinate dehydrogenase complex from Bacillus subtilis membranes
(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
- Hederstedt, Lars LU and Andersson, K Kristoffer
- publishing date
- 1986
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Bacteriology
- volume
- 167
- issue
- 2
- pages
- 735 - 739
- publisher
- American Society for Microbiology
- external identifiers
-
- scopus:0022525547
- 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
- 2024-01-14 00:58:28
@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}}, doi = {{10.1128/jb.167.2.735-739.1986}}, volume = {{167}}, year = {{1986}}, }