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Chlorophyll-based phototrophs, or chlorophototrophs, convert light energy into stored chemical potential energy using two types of photochemical reaction center (RC), denoted type-1 and type-2. After excitation with light, a so-called special pair of chlorophylls in the RC is oxidized, and an acceptor is reduced. To ensure that RCs function at maximal rates in diffuse and variable light conditions, chlorophototrophs have independently evolved diverse light-harvesting antenna systems to rapidly and efficiently transfer that energy to the RCs. Energy transfer between weakly coupled chromophores is generally believed to proceed by resonance energy transfer, a dipole-induced-dipole process that was initially described theoretically by Förster. Nature principally optimizes three parameters in antenna systems: the distance separating the donor and acceptor chromophores, the relative orientations of those chromophores, and the spectral overlap between the donor and the acceptor chromophores. However, there are other important biological parameters that nature has optimized, and some common themes emerge from comparisons of different antenna systems. This tutorial considers structural and functional characteristics of three fundamentally different light-harvesting antenna systems of chlorophotrophic bacteria: phycobilisomes of cyanobacteria, the light-harvesting complexes (LH1 and LH2) of purple bacteria, and chlorosomes of green bacteria. Phycobilisomes are generally considered to represent an antenna system in which the chromophores are weakly coupled, while the strongly coupled bacteriochlorophyll molecules in LH1 and LH2 are strongly coupled and are better described by exciton theory. Chlorosomes can contain up to 250 000 bacteriochlorophyll molecules, which are very strongly coupled and form supramolecular, nanotubular arrays. The general and specific principles that have been optimized by natural selection during the evolution of these diverse light-harvesting antenna systems are discussed. [ABSTRACT FROM AUTHOR]

A fourth and large family of lycopene cyclases was identified in photosynthetic prokaryotes. The first member of this family, encoded by the cruA gene of the green sulfur bacterium Chlorobium tepidum. was identified in a complementation assay with a lycopene-producing strain of Escherichia coil. Orthologs of cruA are found in all available green sulfur bacterial genomes and in all cyanobacterial genomes that lack genes encoding CrtL- or CrtY-type lycopene cyclases. The cyanobacterium Synechococcus sp. PCC 7002 has two homologs of CruA. denoted CruA and CruP, and both were shown to have lycopene cyclase activity. Although all characterized lycopene cyclases in plants are CrtL-type proteins, genes orthologous to cruP also occur in plant genomes. The CruA- and CruP-type carotenoid cyclases are members of the FixC dehydrogenase superfamily and are distantly related to CrtL- and CrtY-type lycopene cyclases. Identification of these cyclases fills a major gap in the carotenoid biosynthetic pathways of green sulfur bacteria and cyanobacteria. [ABSTRACT FROM AUTHOR]