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Biophys J, September 2000, p. 1171-1179, Vol. 79, No. 3


*Dip. Chimica, Università di Bari, I-70126 Bari;
CS-CFILM (CNR), Bari;
Dip. Chimica,
Università "La Sapienza," Roma; §CSGI-Dip.
Chimica, Università di Firenze, Firenze; ¶Lab.
Biochimica Biofisica, Dip. Biologia, Università di Bologna,
Bologna, Italy
The kinetics of charge recombination between the primary
photoxidized donor (P+) and the secondary reduced quinone
acceptor (QB
) have been studied in reaction centers
(RCs) from the purple photosynthetic bacterium Rhodobacter
sphaeroides incorporated into lecithin vesicles containing large
ubiquinone pools over the temperature range 275 K
T
307 K. To account for the non-exponential kinetics of P+
re-reduction observed following a flash, a new approach has been developed, based on the following assumptions: 1) the exchange of
quinone between different vesicles is negligible; 2) the exchange of
quinone between the QB site of the RC and the quinone pool within each single vesicle is faster than the return of the electron from the primary reduced acceptor QA
to
P+; 3) the size polydispersity of proteoliposomes and the
distribution of quinone molecules among them result in a quinone
concentration distribution function, P(Q). The first and second moments
of P(Q) have been evaluated from the size distribution of
proteoliposomes probed by quasi-elastic light scattering (mean radius,
R
= (50 ± 15) nm). Following these premises, we describe
the kinetics of P+QB
recombination with a
truncated cumulant expansion and relate it to P(Q) and to the free
energy changes for QA
QB
QAQB
electron transfer
(
GABo) and for quinone binding
(
Gbindo) at QB. The model
accounts well for the temperature and quinone dependence of the charge
recombination kinetics, yielding
GABo =
7.67 ± 0.05 kJ mol
1 and
Gbindo =
14.6 ± 0.6 kJ
mol
1 at 298 K.
Biophys J, September 2000, p. 1171-1179, Vol. 79, No. 3
© 2000 by the Biophysical Society 0006-3495/00/09/1171/09 $2.00
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