期刊
PHOTOSYNTHESIS RESEARCH
卷 120, 期 1-2, 页码 87-98出版社
SPRINGER
DOI: 10.1007/s11120-013-9821-6
关键词
X-ray diffraction; Protein purification; Spectroscopy; Membrane protein; Rhodobacter sphaeroides; Blastochloris viridis
资金
- National Science Foundation [CHE 1158552]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1158552] Funding Source: National Science Foundation
This review presents a broad overview of the research that enabled the structure determination of the bacterial reaction centers from Blastochloris viridis and Rhodobacter sphaeroides, with a focus on the contributions from Duysens, Clayton, and Feher. Early experiments performed in the laboratory of Duysens and others demonstrated the utility of spectroscopic techniques and the presence of photosynthetic complexes in both oxygenic and anoxygenic photosynthesis. The laboratories of Clayton and Feher led efforts to isolate and characterize the bacterial reaction centers. The availability of well-characterized preparations of pure and stable reaction centers allowed the crystallization and subsequent determination of the structures using X-ray diffraction. The three-dimensional structures of reaction centers revealed an overall arrangement of two symmetrical branches of cofactors surrounded by transmembrane helices from the L and M subunits, which also are related by the same twofold symmetry axis. The structure has served as a framework to address several issues concerning bacterial photosynthesis, including the directionality of electron transfer, the properties of the reaction center-cytochrome c (2) complex, and the coupling of proton and electron transfer. Together, these research efforts laid the foundation for ongoing efforts to address an outstanding question in oxygenic photosynthesis, namely the molecular mechanism of water oxidation.
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