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

Henrik Fridén; Myles R. Cheesman; Lars Hederstedt; Kristoffer K. Andersson; Andrew J. Thomson

doi:10.1016/0167-4838(90)90067-P

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

Henrik Fridén, Myles R. Cheesman, Lars Hederstedt, Kristoffer K. Andersson, Andrew J. Thomson

Research output: Contribution to journal › Article › peer-review

35 Citations (Scopus)

Original language	English
Pages (from-to)	207-215
Journal	Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Volume	1041
Issue number	2
DOIs	https://doi.org/10.1016/0167-4838(90)90067-P
Publication status	Published - 15 Nov 1990

Keywords

EPR
Succinate
quinone oxidoreductase
Heme iron
(B. subtilis)

Access to Document

10.1016/0167-4838(90)90067-P

Cite this

Fridén, H., Cheesman, M. R., Hederstedt, L., Andersson, K. K., & Thomson, A. J. (1990). 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. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1041(2), 207-215. https://doi.org/10.1016/0167-4838(90)90067-P

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keywords = "EPR, Succinate, quinone oxidoreductase, Heme iron, (B. subtilis)",

author = "Henrik Frid{\'e}n and Cheesman, {Myles R.} and Lars Hederstedt and Andersson, {Kristoffer K.} and Thomson, {Andrew J.}",

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Fridén, H, Cheesman, MR, Hederstedt, L, Andersson, KK & Thomson, AJ 1990, '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', Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol. 1041, no. 2, pp. 207-215. https://doi.org/10.1016/0167-4838(90)90067-P

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, Henrik; Cheesman, Myles R.; Hederstedt, Lars et al.

In: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, Vol. 1041, No. 2, 15.11.1990, p. 207-215.

Research output: Contribution to journal › Article › peer-review

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AU - Fridén, Henrik

AU - Cheesman, Myles R.

AU - Hederstedt, Lars

AU - Andersson, Kristoffer K.

AU - Thomson, Andrew J.

PY - 1990/11/15

Y1 - 1990/11/15

KW - EPR

KW - Succinate

KW - quinone oxidoreductase

KW - Heme iron

KW - (B. subtilis)

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DO - 10.1016/0167-4838(90)90067-P

M3 - Article

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SP - 207

EP - 215

JO - Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

JF - Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

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Fridén H, Cheesman MR, Hederstedt L, Andersson KK, Thomson AJ. 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. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1990 Nov 15;1041(2):207-215. doi: 10.1016/0167-4838(90)90067-P