Ongoing questions surround the influence of protein dynamics on rapid processes such as biological electron transfer. Such questions are particularly addressable in light-activated systems. In Rhodobacter sphaeroides reaction centers, charge recombination or back electron transfer from the reduced bacteriopheophytin, H-A(-), to the oxidized dimeric bacteriochlorophyll, P+, may be monitored by both transient absorption spectroscopy and transient fluorescence spectroscopy. Signals measured with both these techniques decay in a similar three-exponential fashion with lifetimes of similar to 0.6-0.7, similar to 2-4, and similar to 10-20 ns, revealing the complex character of this electron transfer reaction. In this study a single kinetic model was developed to connect lifetime and amplitude data from both techniques. The model took into account the possibility that electron transfer from H-A(-) to P+ may occur with transient formation of the state P+BA-. As a result it was possible to model the impact of nanosecond protein relaxation on the free energy levels of both P+HA- and P+BA- states relative to that of the singlet excited state of P, P*. Surprisingly, whereas the free energy gap between P* and P+HA- increased with time in response to protein reorganization, the free energy gap between P* and P+BA- decreased. This finding may be accounted for by a gradual polarization of the protein environment which stabilizes the state P+HA- and destabilizes the state P+BA-, favoring productive charge separation over unproductive charge recombination.