Protein dielectric relaxations in photosynthetic reaction centers associated with the primary charge separation: evidence coming from photovoltage measurements

摘要

The X-ray crystallographic analysis of the bacterial reaction center suggests a rigid and immobile structure (Deisenhofer et al., 1984). However, proteins are known to fluctuate substancially around an average structure (Frauenfelder et al., 1979). At room temperature proteins can assume many nearly isoenergetic conformational substates which are separated by energy barriers varying widely in height. Accordingly, the transitions between the substates occurs on time scales spread over many orders ofmagnitude.