Quinol oxidation by the ubiquinol:cytochrome c(2) oxidoreductase in the chromatophores from Rhodobacter sphaeroides
Wang, Zhenggan
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https://hdl.handle.net/2142/19323
Description
Title
Quinol oxidation by the ubiquinol:cytochrome c(2) oxidoreductase in the chromatophores from Rhodobacter sphaeroides
Author(s)
Wang, Zhenggan
Issue Date
1990
Doctoral Committee Chair(s)
Crofts, Antony R.
Department of Study
Biophysics and Computational Biology
Discipline
Biophysics
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biophysics, General
Language
eng
Abstract
The kinetics and thermodynamics of the high potential chain in the chromatophores from Rhodobacter sphaeroides have been reexamined. It was found that RC, cyt c$\sb2$ and c$\sb1$ after a flash reached a state not far from the expected ideal equilibrium under the conditions of our experiments.
An extinction coefficient for cyt b$\sb{\rm H}$ was computed from comparison of oxidation kinetics of c cytochromes in the presence of antimycin and UHDBT. The effects of myxothiazol on the cyt c oxidation have also been discussed.
Our observations of the temperature dependence of cyt b reduction suggested that quinone diffusion was more rapid than turnover of the bc$\sb1$ complex, and that the chemical step of quinol oxidation was the rate-limiting step in the photosynthetic electron transport of chromatophore system.
Oxidation kinetic of quinol by bc$\sb1$ complex in chromatophores was simulated. A set of kinetic parameters were obtained from optimization, and compared with experimental results. A minimal model of quinol oxidation was proposed, and discussed under the context of the Q-cycle mechanism.
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