Although the three-dimensional structure of the bacterial photosynthet
ic reaction center (RC) reveals a high level of structural symmetry, w
ith two nearly equivalent potential electron transfer pathways, the RC
is functionally asymmetric: Electron transfer occurs along only one o
f the two possible pathways. In order to determine the origins of this
symmetry breaking, the internal electric field present in the RC when
charge is separated onto structurally characterized sites was probed
by using absorption band shifts of the chromophores within the RC. The
sensitivity of each probe chromophore to an electric field was calibr
ated by measuring the Stark effect spectrum, the change in absorption
due to an externally applied electric field. A quantitative comparison
of the observed absorption band shifts and those predicted from vacuu
m electrostatics gives information on the effective dielectric constan
t of the protein complex. These results reveal a significant asymmetry
in the effective dielectric strength of the protein complex along the
two potential electron transfer pathways, with a substantially higher
dielectric strength along the functional pathway. This dielectric asy
mmetry could be a dominant factor in determining the functional asymme
try of electron transfer in the RC.