Isolation, photosynthetic reaction centers

Woodbury, N. W. T., and Parson, W. W., 1984, Nanosecond fluorescence from isolated photosynthetic reaction centers of Rhodopseudomonas sphaeroides. Biochim. Biophys. Acta, 767 345n361. 

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Michel, H., et al. The "heavy" subunit of the photosynthetic reaction center from Rhodopseudomonas viridis isolation of the gene, nucleotide and amino acid sequence. EMBO J. 4 1667-1672, 1985. 

Van der Rest, M. and Gingras, G. 1974. The pigment complement of the photosynthetic reaction center isolated from Rhodospirillum rubrum. J. Biol. Chem., 249,6446-6453. 

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Proteins that have tightly bound cofactors, such as heme proteins, photosynthetic reaction centers and antenna proteins, flavoproteins, and pyridoxal phosphate- and NAD-dependent enzymes, provide a variety of chromophores which have absorption bands in the visible and UV region. The CD bands associated with the chromophoric groups are frequently quite intense, despite the fact that the isolated chromophores are achiral in many cases, and therefore have no CD, or are separated from the nearest chiral center by several bonds about which relatively free rotation can occur, and therefore have only weak CD. The extrinsic or induced CD observed in the visible and near-UV spectra of the proteins can provide useful information about the conformation and/or environment of the bound chromophore, which usually plays a critical role in the function of the protein. 

The bacterial photosynthetic reaction center (RC) of Rps. sphaeroides is composed of three protein subunits called L, M, H, having the respective molecular weight of 28000, 32000, 36000 as determined from the amino acid compositions (1). After isolation of the RC, the H subunit can be removed and all of the chromophores remain in the final LM complex which is still fully functional with respect to the primary light-induced reactions (1-3). 

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