Electron transfer and protein dynamics in the photosynthetic reaction center

Benjamin H. McMahon, Joachim D. Müller, Colin A. Wraight, G. Ulrich Nienhaus

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178 Scopus citations


We have measured the kinetics of electron transfer (ET) from the primary quinone (Q(A)) to the special pair (P) of the reaction center (RC) complex from Rhodobacter sphaeroides as a function of temperature (5-300 K), illumination protocol (cooled in the dark and under illumination from 110, 160, 180, and 280 K), and warming rate (1.3 and 13 mK/s). The nonexponential kinetics are interpreted with a quantum-mechanical ET model (Fermi's golden rule and the spin-boson model), in which heterogeneity of the protein ensemble, relaxations, and fluctuations are cast into a single coordinate that relaxes monotonically and is sensitive to all types of relaxations caused by ET. Our analysis shows that the structural changes that occur in response to ET decrease the free energy gap between donor and acceptor states by 120 meV and decrease the electronic coupling between donor and acceptor states from 2.7 x 10-4 cm-1 to 1.8 x 10-4 cm-1. At cryogenic temperatures, conformational changes can be slowed or completely arrested, allowing us to monitor relaxations on the annealing time scale (~103-104 s) as well as the time scale of ET (~100 ms). The relaxations occur within four broad tiers of conformational substates with average apparent Arrhenius activation enthalpies of 17, 50, 78, and 110 kJ/mol and preexponential factors of 1013, 1015, 1021, and 1025 s-1, respectively. The parameterization provides a prediction of the time course of relaxations at all temperatures. At 300 K, relaxations are expected to occur from 1 ps to 1 ms, whereas at lower temperatures, even broader distributions of relaxation times are expected. The weak dependence of the ET rate on both temperature and protein conformation, together with the possibility of modeling heterogeneity and dynamics with a single conformational coordinate, make RC a useful model system for probing the dynamics of conformational changes in proteins.

Original languageEnglish (US)
Pages (from-to)2567-2587
Number of pages21
JournalBiophysical journal
Issue number5
StatePublished - May 1998
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported by the National Institutes of Health (grants PHS2 R01 GM 18051 and PHS5 T32 GM 08276) and the National Science Foundation (grants PHY95-13217 and IMCB 96-31063).


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