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In many electron-transfer proteins, the arrangement of cofactors implies a succession of uphill and downhill steps. The kinetic implications of such arrangements are examined in the present work, based on a study of chimeric photosynthetic reaction centers obtained by expressing the tetraheme subunit from Blastochloris viridis in another purple bacterium, Rubrivivax gelatinosus. Site-directed mutations of the environment of heme c559, which is the immediate electron donor to the primary donor P, induced modifications of this heme's midpoint potential over a range of 400 mV. This resulted in shifts of the apparent midpoint potentials of the neighboring carriers, yielding estimates of the interactions between redox centers. At both extremities of the explored range, the energy profile of the electron-transfer chain presented an additional uphill step, either downstream or upstream from c559. These modifications caused conspicuous changes of the electron-transfer rate across the tetraheme subunit, which became approximately 100-fold slower in the mutants where the midpoint potential of c559 was lowest. A theoretical analysis of the kinetics is presented, predicting a displacement of the rate-limiting step when lowering the potential of c559. A reasonable agreement with the data was obtained when combining this treatment with the rates predicted by electron transfer theory for the individual rate constants.
Alric et al. (Wed,) studied this question.