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Low temperature EPR and MCD studies on cytochrome b-558 of the Bacillus subtilis succinate: quinone oxidoreductase indicate bis-histidine coordination of the heme iron

Fridén, H; Cheesman, MR; Hederstedt, Lars LU ; Andersson, K Kristoffer and Thomson, Andrew J. (1990) In Biochimica et Biophysica Acta - Bioenergetics 1041(2). p.207-215
Abstract
Bacillus subtilis cytochrome b-558 was expressed in high amounts in Escherichia coli, solubilized from membranes with detergent and purified free from other hemoproteins. The cytochrome possibly contains two heme groups. To determine the axial ligands to the low-spin heme and the heme rhombicity, the cytochrome was analyzed using low-temperature electron paramagnetic resonance (EPR) and magnetic circular dichroism (MCD) spectroscopy. The combined results exclude bis-methionine, bis-lysine and histidine-methionine coordination. Bis-histidine coordination of the heme(s) with a near perpendicular orientation of the imidazole planes is strongly suggested by the highly axial low-spin EPR signals and the intense near infrared MCD spectrum... (More)
Bacillus subtilis cytochrome b-558 was expressed in high amounts in Escherichia coli, solubilized from membranes with detergent and purified free from other hemoproteins. The cytochrome possibly contains two heme groups. To determine the axial ligands to the low-spin heme and the heme rhombicity, the cytochrome was analyzed using low-temperature electron paramagnetic resonance (EPR) and magnetic circular dichroism (MCD) spectroscopy. The combined results exclude bis-methionine, bis-lysine and histidine-methionine coordination. Bis-histidine coordination of the heme(s) with a near perpendicular orientation of the imidazole planes is strongly suggested by the highly axial low-spin EPR signals and the intense near infrared MCD spectrum (Δϵ=380 M−1·cm−1 at 4.2 K and 5 T) of the charge-transfer band at 1600 nm. (Less)
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Contribution to journal
publication status
published
subject
in
Biochimica et Biophysica Acta - Bioenergetics
volume
1041
issue
2
pages
207 - 215
publisher
Elsevier
ISSN
0005-2728
DOI
10.1016/0167-4838(90)90067-P
language
English
LU publication?
yes
id
e16afce5-7f16-4b9d-850f-4908b58a85c8
date added to LUP
2017-07-18 10:39:20
date last changed
2017-09-07 10:03:45
@article{e16afce5-7f16-4b9d-850f-4908b58a85c8,
  abstract     = {Bacillus subtilis cytochrome b-558 was expressed in high amounts in Escherichia coli, solubilized from membranes with detergent and purified free from other hemoproteins. The cytochrome possibly contains two heme groups. To determine the axial ligands to the low-spin heme and the heme rhombicity, the cytochrome was analyzed using low-temperature electron paramagnetic resonance (EPR) and magnetic circular dichroism (MCD) spectroscopy. The combined results exclude bis-methionine, bis-lysine and histidine-methionine coordination. Bis-histidine coordination of the heme(s) with a near perpendicular orientation of the imidazole planes is strongly suggested by the highly axial low-spin EPR signals and the intense near infrared MCD spectrum (Δϵ=380 M−1·cm−1 at 4.2 K and 5 T) of the charge-transfer band at 1600 nm.},
  author       = {Fridén, H and Cheesman, MR and Hederstedt, Lars and Andersson, K Kristoffer and Thomson, Andrew J.},
  issn         = {0005-2728},
  language     = {eng},
  number       = {2},
  pages        = {207--215},
  publisher    = {Elsevier},
  series       = {Biochimica et Biophysica Acta - Bioenergetics},
  title        = {Low temperature EPR and MCD studies on cytochrome <em>b</em>-558 of the <em>Bacillus subtilis</em> succinate: quinone oxidoreductase indicate bis-histidine coordination of the heme iron},
  url          = {http://dx.doi.org/10.1016/0167-4838(90)90067-P},
  volume       = {1041},
  year         = {1990},
}