Steady-state cyclic electron transfer through solubilized Rhodobacter sphaeroides reaction centres
(2000) In Biophysical Chemistry 88(1-3). p.137-152- Abstract
- The mechanism, thermodynamics and kinetics of light-induced cyclic electron transfer have been studied in a model energy-transducing system consisting of solubilized Rhodobacter sphaeroides reaction center/light harvesting-1 complexes (so-called core complexes), horse heart cytochrome c and a ubiquinone-0/ubiquinol-0 pool. An analysis of the steady-state kinetics of cytochrome c reduction by ubiquinol-0, after a light-induced steady-state electron flow had been attained, showed that the rate of this reaction is primarily controlled by the one-electron oxidation of the ubiquinol-anion. Re-reduction of the light-oxidized reaction center primary donor by cytochrome c was measured at different reduction levels of the ubiquinone-0/ubiquinol-0... (More)
- The mechanism, thermodynamics and kinetics of light-induced cyclic electron transfer have been studied in a model energy-transducing system consisting of solubilized Rhodobacter sphaeroides reaction center/light harvesting-1 complexes (so-called core complexes), horse heart cytochrome c and a ubiquinone-0/ubiquinol-0 pool. An analysis of the steady-state kinetics of cytochrome c reduction by ubiquinol-0, after a light-induced steady-state electron flow had been attained, showed that the rate of this reaction is primarily controlled by the one-electron oxidation of the ubiquinol-anion. Re-reduction of the light-oxidized reaction center primary donor by cytochrome c was measured at different reduction levels of the ubiquinone-0/ubiquinol-0 pool. These experiments involved single turnover flash excitation on top of background illumination that elicited steady-state cyclic electron transfer. At low reduction levels of the ubiquinone-0/ubiquinol-0 pool, the total cytochrome c concentration had a major control over the rate of reduction of the primary donor. This control was lost at higher reduction levels of the ubiquinone/ubiquinol-pool, and possible reasons for this behaviour are discussed. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/125223
- author
- van Rotterdam, Bart LU ; Westerhoff, Hans V ; Visschers, Ronald W ; Jones, Michael R ; Hellingwerf, Klaas J and Crielaard, Wim
- organization
- publishing date
- 2000
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Rhodobacter sphaeroides, Reaction center, Electron transfer, Ubiquinone, Cytochrome c, Control theory
- in
- Biophysical Chemistry
- volume
- 88
- issue
- 1-3
- pages
- 137 - 152
- publisher
- Elsevier
- external identifiers
-
- scopus:0034672774
- ISSN
- 1873-4200
- DOI
- 10.1016/S0301-4622(00)00206-4
- language
- English
- LU publication?
- yes
- id
- c6012212-2287-4351-8a9c-1449bcb4755d (old id 125223)
- date added to LUP
- 2016-04-01 16:25:30
- date last changed
- 2025-10-14 12:22:25
@article{c6012212-2287-4351-8a9c-1449bcb4755d,
abstract = {{The mechanism, thermodynamics and kinetics of light-induced cyclic electron transfer have been studied in a model energy-transducing system consisting of solubilized Rhodobacter sphaeroides reaction center/light harvesting-1 complexes (so-called core complexes), horse heart cytochrome c and a ubiquinone-0/ubiquinol-0 pool. An analysis of the steady-state kinetics of cytochrome c reduction by ubiquinol-0, after a light-induced steady-state electron flow had been attained, showed that the rate of this reaction is primarily controlled by the one-electron oxidation of the ubiquinol-anion. Re-reduction of the light-oxidized reaction center primary donor by cytochrome c was measured at different reduction levels of the ubiquinone-0/ubiquinol-0 pool. These experiments involved single turnover flash excitation on top of background illumination that elicited steady-state cyclic electron transfer. At low reduction levels of the ubiquinone-0/ubiquinol-0 pool, the total cytochrome c concentration had a major control over the rate of reduction of the primary donor. This control was lost at higher reduction levels of the ubiquinone/ubiquinol-pool, and possible reasons for this behaviour are discussed.}},
author = {{van Rotterdam, Bart and Westerhoff, Hans V and Visschers, Ronald W and Jones, Michael R and Hellingwerf, Klaas J and Crielaard, Wim}},
issn = {{1873-4200}},
keywords = {{Rhodobacter sphaeroides; Reaction center; Electron transfer; Ubiquinone; Cytochrome c; Control theory}},
language = {{eng}},
number = {{1-3}},
pages = {{137--152}},
publisher = {{Elsevier}},
series = {{Biophysical Chemistry}},
title = {{Steady-state cyclic electron transfer through solubilized Rhodobacter sphaeroides reaction centres}},
url = {{http://dx.doi.org/10.1016/S0301-4622(00)00206-4}},
doi = {{10.1016/S0301-4622(00)00206-4}},
volume = {{88}},
year = {{2000}},
}