PubMed1998
The photosynthetic reaction center of Rhodopseudomonas viridis, a purple bacterium, contains a tetraheme cytochrome subunit. After its photoinduced oxidation, the primary donor, P, is reduced by the nearby heme (c559) of the tetraheme subunit in about 200 ns. This heme, in turn, is reduced by another heme (c556) of the subunit in about 2 micro(s). The midpoint potentials of P, c559, and c556 are known to be +500, +380, and +320 mV, respectively. The reduction kinetics of P+ are strongly biphasic in living cells, membrane fragments, and isolated reaction centers. We show here that this biphasicity reflects a small equilibrium constant (lower than 10) for the electron-transfer reaction between P and c559, which arises from a significant difference between the operating redox potentials of the P+/P and c559+/c559 couples and their equilibrium midpoint potentials. This difference is partly due to the effect of the permanent transmembrane potential, which arises from the cell metabolism, and to significant electrostatic interactions which develop between the electron carriers of the reaction center. Interestingly, the kinetic parameters of P+ reduction in decoupled cells or membrane fragments are identical to those reported for isolated reaction centers. We estimate an interaction of about 20 mV between c556 and c559 and about 90 mV between c559 and P. Consequently, the operating redox potential of the P+/P couple is 410 mV.