This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Photosynthetic reaction centers (RC) are integral membrane protein-pigment complexes that perform light induced electron transfer from a bacteriochlorophyll dimer (D) to two quinone molecules QA and QB. The RC forms a complex with another pigment-containing integral membrane protein called the light-harvesting complex (LH1) whose primary function is to gather light and transfer this energy to the RC and photo-oxidize D. In addition, a 14-kilodalton water soluble-cytochrome c2 transiently binds to the RC and re-reduces D. Our ongoing work at SSRL will focus on three structure-function aspects of the RC: 1). Determination of the structure of the RC complexed with other proteins: a). RC and light harvesting protein (LH1), and b). mutants that affect the binding and electron transfer between RC with cyt c2. 2). Determination of the structures of mutants that affect proton and electron transfer events in the RC. 3). Determination of the structures at an enhanced resolution of intermediates that are involved in the charge separation, including D+QA-, D+QB-, and the biradical intermediate state DQA-QB-.
Showing the most recent 10 out of 604 publications
