Bacteriochlorophyll protein

Twofold contacts are self-homologous—formed by equivalent surfaces from each of the participating subunits, while the occasional 3-fold (e.g., bacteriochlorophyll protein), 4-fold (hemerythrin), or 17-fold (tobacco mosaic virus) contact is heterologous—formed by joining two different surfaces. An especially interesting type of het-... [Pg.244]

Glyceraldehyde-phosphate dehydrogenase domain 2 Bacteriochlorophyll protein p-Hydroxybenzoate hydroxylase domain 2 Influenza virus hemagglutinin HA2 L7/L12 ribosomal protein... [Pg.259]

Azurin (Adman et ah, 1978), see Plastocyanin Bacteriochlorophyll protein (B. W. Matthews et ah, 1979) Open-face fi sandwich (Fig. 83)... [Pg.278]

R Emerson and W Arnold (1932) The photochemical reaction in photosynthesis. J Gen Physiol 16 191-205 Govindjee (1999) On the requirement of minimum number of four versus eight quanta of light for the evolution of one molecule of oxygen in photosynthesis A historical note. Photosynthesis Res 59 249-254 RE Fenna, BW Mathews, JM Olson and EK Shaw (1974) Structure of a bacteriochlorophyll-protein from the green photosynthetic bacterium Chlorobium limicola crystallographic evidence fora trimer. J Mol Biol 84 231 -240... [Pg.45]

K Sauer and LA Austin (1978) Bacteriochlorophyll-protein complexes from the light-harvesting antenna of the photosynthetic bacteria. Biochemistry 17 2011-2019... [Pg.84]

R5. BW Mathews, and RE Fenna (1980) Structure of a green bacteriochlorophyll protein. Accts Chem. Res. 13 309-317. [Pg.157]

KD Philipson and K Sauer (1972) Exciton interaction in a bacteriochlorophyll-protein from Chloropseudomonas ethylica. Absorption and circular dichroism at 77 K. Biochemistry 11 1880-1885... [Pg.158]

RE Fenna, BW Mathews, JM Olson and EK Shaw (1974) Structure of a bacteriochlorophyll-protein from the green photosynthetic bacterium Chlorobium limicola-. Crystallographic evidence fora trimer. J Mol Biol 84 231 -240... [Pg.158]

CD measurements at 77 °K of a bacteriochlorophyll protein from Chloropseudomonas ethylica indicated exciton splitting near 800 and 600 nm of bacteriochlorophyll a molecules. Distances of 12—15 A between the interacting molecules in a protein subunit were estimated (269). [Pg.105]

Prince SM, Papiz, MZ, Freer AA, McDermott G, Hawthornthwaite-Lawless AM, Cogdell RJ and Isaacs NW (1977) Apoprotein structure in the LH2 complex from Rhodopseudomonas acidophila strain 10050 Modular assembly and protein pigment interactions. J Mol Biol 268 412-423 Pullerits T and Sundstrom V (1996) Photosynthetic lightharvesting pigment-protein complexes Toward understanding how and why. Acc Chem Res 29 381-389 Robert B and Lutz M (1985) Structure of anterma complexes of several Rhodospirillales from their resonance Raman spectra. Biochim Biophys Acta 807 10-23 Sauer K, Cogdell RJ, Prince SM, Freer AA, Isaacs NW and Scheer H (1996) Structure based calculations ofthe optical spectra ofthe LH2 bacteriochlorophyll-protein complex from Rhodopseudomonas acidophila. Photochem Photobiol 64 564-576... [Pg.80]

Noy D, Moser CC, and Dutton PL. Bacteriochlorophyll protein maquettes. In Biochemistry and Biophysics of Chlorophylls, edited by Grimm B, Porra R, Rudiger W, and Scheer H. Kluwer Academic, New York, 2004. [Pg.63]

Alden RG, Johnson E, Nagarajan V, Parson WW, Law CJ and Cogdell RJ. Calculations of the spectroscopic properties of the LH2 bacteriochlorophyll-protein antenna complex from Rhodopseudomonas acidophila. J. Phys. ChemB. 1996 101 4667-4680. [Pg.87]

Olson JM (1978) Bacteriochlorophyll -proteins from green bacteria. In Clayton RK and Sistrom WR, eds. The Photosynthetic Bacteria, pp. 161-178. New York-London Plenum Press. [Pg.184]

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