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
(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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https://lup.lub.lu.se/record/e16afce5-7f16-4b9d-850f-4908b58a85c8
- author
- Fridén, H ; Cheesman, MR ; Hederstedt, Lars LU ; Andersson, K Kristoffer and Thomson, Andrew J.
- organization
- publishing date
- 1990
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochimica et Biophysica Acta - Bioenergetics
- volume
- 1041
- issue
- 2
- pages
- 207 - 215
- publisher
- Elsevier
- external identifiers
-
- scopus:0025009144
- 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
- 2021-01-03 09:01:47
@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}},
doi = {{10.1016/0167-4838(90)90067-P}},
volume = {{1041}},
year = {{1990}},
}