PROPERTIES OF SINGLE ASSEMBLIES OF LIGHT HARVESTER LH2

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. We are examining the photobleaching and transfer dynamics in single assemblies of the LH2 complexes and the up-dipeptides that can be reversibly extracted from them. Each LH2 contains eighteen bacteriochlorophylls (B850) and nine collectors (B800). The fluorescence lifetimes, polarization, correlation times and bleaching kinetics are being studied under a variety of conditions. The primary goals include measurements of long time scale protein dynamics. Previous polarization experiments have revealed conformational dynamics associated with excitonic migration in the monomeric LH2 assembly. Furthermore, blue emission originating from higher excited states was recently detected and investigated.