Biochimica et Biophysica Acta (BBA) - Bioenergetics
Volume 1459, Issues 2–3, 15 August 2000, Pages 456-466
Proton-coupled electron transfer at the Qo site: what type of mechanism can account for the high activation barrier?
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Keywords
Myxothiazol
Stigmatellin
Activation energy
Mutagenesis
Proton-coupled electron transfer
Abbreviations
cyt, cytochrome
cyt bH, the higher potential heme of cyt b
cyt bL, the lower potential heme of cyt b
ES, enzyme-substrate
ET, electron transfer
ISP, iron-sulfur protein
ISPox, H-ISPred, oxidized and reduced forms of ISP
MOA-, methoxyacrylate
-PEWY-, conserved span of cyt b, starting with Pro-271 in bovine sequence, with the sequence in single-letter code
PT, proton transfer
Q, quinone
QH2, hydroquinone or quinol
Qi site, quinone reducing site
Qo site, hydroquinone oxidizing site
SQ-ISP, putative complex between semiquinone and ISP
Cited by (0)
- 1
Present address: Service de Photosynthèse, Institut de Biologie Physico-Chimique, 13, rue Pierre et Marie Curie, 75005 Paris, France.
- 2
Present address: Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104-6059, USA.
- 3
Present address: Department of Biological Chemistry, Johns Hopkins University, School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA.
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