Effects of temperature and ΔG°on electron transfer from cytochrome c2 to the photosynthetic reaction center of the purple bacterium Rhodobacter sphaeroides

G. Venturoli, F. Drepper, J. C. Williams, James Paul Allen, X. Lin, P. Mathis

Research output: Contribution to journalArticle

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Abstract

The kinetics of electron transfer from cytochrome c2 to the primary donor (P) of the reaction center from the photosynthetic purple bacterium Rhodobacter sphaeroides have been investigated by time-resolved absorption spectroscopy. Rereduction of P+ induced by a laser pulse has been measured at temperatures from 300 K to 220 K in a series of specifically mutated reaction centers characterized by altered midpoint redox potentials of P+/P varying from 410 mV to 765 mV (as compared to 505 mV for wild type). Rate constants for first-order electron donation within preformed reaction center- cytochrome c2 complexes and for the bimolecular oxidation of free cytochrome c2 have been obtained by multiexponential deconvolution of the kinetics. At all temperatures the rate of the fastest intracomplex electron transfer increases by more than two orders of magnitude as the driving force -ΔG°is varied over a range of 350 meV. The temperature and ΔG°dependences of the rate constant fit the Marcus equation well. Global analysis yields a reorganization energy λ = 0.96 ± 0.07 eV and a set of electronic matrix elements, specific for each mutant, ranging from 1.2 10-4 eV to 2.5 10-4 eV. Analysis in terms of the Jortner equation indicates that the best fit is obtained in the classical limit and restricts the range of coupled vibrational modes to frequencies lower than ~200 cm-1. An additional slower kinetic component of P+ reduction, attributed to electron transfer from cyt c2 docked in a nonoptimal configuration of the complex, displays a Marcus type dependence of the rate constant upon ΔG°, characterized by a similar value of λ (0.8 ± 0.1 eV) and by an average electronic matrix element smaller by more than one order of magnitude. In all of the mutants, as the temperature is decreased below 260 K, both intracomplex reactions are abruptly inhibited, their rate being negligible at 220 K. The free energy dependence of the second-order rate constant for oxidation of cyt c2 in solution suggests that the collisional reaction is partially diffusion controlled, reaching the diffusion limit at exothermicities between 150 and 250 meV over the temperature range investigated.

Original languageEnglish
Pages (from-to)3226-3240
Number of pages15
JournalBiophysical Journal
Volume74
Issue number6
Publication statusPublished - Jun 1998

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Cytochromes c2
Photosynthetic Reaction Center Complex Proteins
Rhodobacter sphaeroides
Proteobacteria
Electrons
Temperature
Oxidation-Reduction
Spectrum Analysis
Lasers

ASJC Scopus subject areas

  • Biophysics

Cite this

Effects of temperature and ΔG°on electron transfer from cytochrome c2 to the photosynthetic reaction center of the purple bacterium Rhodobacter sphaeroides. / Venturoli, G.; Drepper, F.; Williams, J. C.; Allen, James Paul; Lin, X.; Mathis, P.

In: Biophysical Journal, Vol. 74, No. 6, 06.1998, p. 3226-3240.

Research output: Contribution to journalArticle

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abstract = "The kinetics of electron transfer from cytochrome c2 to the primary donor (P) of the reaction center from the photosynthetic purple bacterium Rhodobacter sphaeroides have been investigated by time-resolved absorption spectroscopy. Rereduction of P+ induced by a laser pulse has been measured at temperatures from 300 K to 220 K in a series of specifically mutated reaction centers characterized by altered midpoint redox potentials of P+/P varying from 410 mV to 765 mV (as compared to 505 mV for wild type). Rate constants for first-order electron donation within preformed reaction center- cytochrome c2 complexes and for the bimolecular oxidation of free cytochrome c2 have been obtained by multiexponential deconvolution of the kinetics. At all temperatures the rate of the fastest intracomplex electron transfer increases by more than two orders of magnitude as the driving force -ΔG°is varied over a range of 350 meV. The temperature and ΔG°dependences of the rate constant fit the Marcus equation well. Global analysis yields a reorganization energy λ = 0.96 ± 0.07 eV and a set of electronic matrix elements, specific for each mutant, ranging from 1.2 10-4 eV to 2.5 10-4 eV. Analysis in terms of the Jortner equation indicates that the best fit is obtained in the classical limit and restricts the range of coupled vibrational modes to frequencies lower than ~200 cm-1. An additional slower kinetic component of P+ reduction, attributed to electron transfer from cyt c2 docked in a nonoptimal configuration of the complex, displays a Marcus type dependence of the rate constant upon ΔG°, characterized by a similar value of λ (0.8 ± 0.1 eV) and by an average electronic matrix element smaller by more than one order of magnitude. In all of the mutants, as the temperature is decreased below 260 K, both intracomplex reactions are abruptly inhibited, their rate being negligible at 220 K. The free energy dependence of the second-order rate constant for oxidation of cyt c2 in solution suggests that the collisional reaction is partially diffusion controlled, reaching the diffusion limit at exothermicities between 150 and 250 meV over the temperature range investigated.",
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N2 - The kinetics of electron transfer from cytochrome c2 to the primary donor (P) of the reaction center from the photosynthetic purple bacterium Rhodobacter sphaeroides have been investigated by time-resolved absorption spectroscopy. Rereduction of P+ induced by a laser pulse has been measured at temperatures from 300 K to 220 K in a series of specifically mutated reaction centers characterized by altered midpoint redox potentials of P+/P varying from 410 mV to 765 mV (as compared to 505 mV for wild type). Rate constants for first-order electron donation within preformed reaction center- cytochrome c2 complexes and for the bimolecular oxidation of free cytochrome c2 have been obtained by multiexponential deconvolution of the kinetics. At all temperatures the rate of the fastest intracomplex electron transfer increases by more than two orders of magnitude as the driving force -ΔG°is varied over a range of 350 meV. The temperature and ΔG°dependences of the rate constant fit the Marcus equation well. Global analysis yields a reorganization energy λ = 0.96 ± 0.07 eV and a set of electronic matrix elements, specific for each mutant, ranging from 1.2 10-4 eV to 2.5 10-4 eV. Analysis in terms of the Jortner equation indicates that the best fit is obtained in the classical limit and restricts the range of coupled vibrational modes to frequencies lower than ~200 cm-1. An additional slower kinetic component of P+ reduction, attributed to electron transfer from cyt c2 docked in a nonoptimal configuration of the complex, displays a Marcus type dependence of the rate constant upon ΔG°, characterized by a similar value of λ (0.8 ± 0.1 eV) and by an average electronic matrix element smaller by more than one order of magnitude. In all of the mutants, as the temperature is decreased below 260 K, both intracomplex reactions are abruptly inhibited, their rate being negligible at 220 K. The free energy dependence of the second-order rate constant for oxidation of cyt c2 in solution suggests that the collisional reaction is partially diffusion controlled, reaching the diffusion limit at exothermicities between 150 and 250 meV over the temperature range investigated.

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