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Rhodopseudomonas acidophila strain

Prince SM, Howard TD, Myles DA, Wilkinson C, Papiz MZ, Freer AA, Cogdell RJ, Isaacs NW. Detergent structure in crystals of the integral membrane light-harvesting complex LH2 from Rhodopseudomonas acidophila strain 10050. J. Mol. Biol. 2003 326 307-315. [Pg.1000]

K. McLuskey, S.M. Prince, R.J. Cogdell, N.W. Isaacs, The crystallographic structure of the B800-820 Lh3 hght-harvesting complex from the purple bacteria Rhodopseudomonas acidophila Strain 7050. Biochem. 40, 8783-8789 (2001)... [Pg.529]

D. Rutkauskas, R. Novoderezkhin, R.J. Cogdell, R. van Grondelle, Fluorescence spectral fluctuations of single LH2 complexes from Rhodopseudomonas acidophila strain 10050. Biochemistry 43, 4431-4438 (2004)... [Pg.531]

H.-M. Wu, N.R.S. Reddy, G. J. Small, Direct observation and hole burning of the lowest exciton level (B870) of the LH2 antenna complex of Rhodopseudomonas acidophila (strain 10050). J. Phys. Chem. B 101, 651-656 (1997b)... [Pg.532]

The Structure and Function of the LH2 Complex from Rhodopseudomonas acidophila Strain 10050, with Special Reference to the Bound Carotenoid... [Pg.71]

In this chapter we shall summarize the structure of the LH2 (B800-850) antenna complex from the purple non-sulfur photosynthetic bacterium Rhodopseudomonas acidophila strain 10050, placing special emphasis on the carotenoids. We will then review what is currently known about the details of the carotenoid s light-harvesting role in this system. [Pg.71]

Fig. 2. The absorption spectrum and CD spectrum of the LH2 complex from Rhodopseudomonas acidophila strain 10050. (a) The abs spectrum of the LH2 complex, (b) A comparison of the abs spectmm (dash line) and the CD spectrum (light line) of the LH2 complex in the visible region of the spectrum, (c) A comparison of the abs spectrum (dash line) and the CD spectrum (light line) of the LH2 complex in the NIR region ofthe spectrum. These data were measured on the BBSRC CD facility at Stirling University, UK with the skilled assistance of Professor Nick Price and Dr Sharon Kelly. Fig. 2. The absorption spectrum and CD spectrum of the LH2 complex from Rhodopseudomonas acidophila strain 10050. (a) The abs spectrum of the LH2 complex, (b) A comparison of the abs spectmm (dash line) and the CD spectrum (light line) of the LH2 complex in the visible region of the spectrum, (c) A comparison of the abs spectrum (dash line) and the CD spectrum (light line) of the LH2 complex in the NIR region ofthe spectrum. These data were measured on the BBSRC CD facility at Stirling University, UK with the skilled assistance of Professor Nick Price and Dr Sharon Kelly.
Fig. 4. A section of the structure of the LH2 complex from Rhodopseudomonas acidophila strain 10050 only showing the pigment. I n Color Plate 5 the representation is B850 BChi a/s - red, B800 BChl a/s - green, rhodopin glucoside - yellow. This figure was redrawn from McDermott et al. (1995). See also Color Plate 5. Fig. 4. A section of the structure of the LH2 complex from Rhodopseudomonas acidophila strain 10050 only showing the pigment. I n Color Plate 5 the representation is B850 BChi a/s - red, B800 BChl a/s - green, rhodopin glucoside - yellow. This figure was redrawn from McDermott et al. (1995). See also Color Plate 5.
Fig. 5. A schematic representation of the arrangement of the pigments in the LH2 complex from Rhodopseudomonas acidophila strain 10050 within one a/3 apoprotein pair. The rhodopin glucoside molecule can be seen coming into contact with the edge of the B800 BCh a molecule and passing over the face of the a-bound B850 BChl a molecule. Fig. 5. A schematic representation of the arrangement of the pigments in the LH2 complex from Rhodopseudomonas acidophila strain 10050 within one a/3 apoprotein pair. The rhodopin glucoside molecule can be seen coming into contact with the edge of the B800 BCh a molecule and passing over the face of the a-bound B850 BChl a molecule.
Fig. 6. A space filling model of the structure of rhodopin-glucoside in the LH2 complex from Rhodopseudomonas acidophila strain 10050. (Top) A side view (Bottom) A view looking down the long axis of the carotenoid. Fig. 6. A space filling model of the structure of rhodopin-glucoside in the LH2 complex from Rhodopseudomonas acidophila strain 10050. (Top) A side view (Bottom) A view looking down the long axis of the carotenoid.
Bissig 1, Brunisholz RA, Cogdell RJ and Zuber H (1988) The complete amino acid sequences of the B800-850 antenna polypeptides from Rhodopseudomonas acidophila strain 7750 Z Naturforsch 43c 77-83... [Pg.79]

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]

CogdeU RJ, Isaacs NW, Freer AA, Arrelano J, Howard TD, Papiz MZ, Hawthornthwaite-Lawless AM and Prince S (1997) The structure and function of the LH2 (B800-850) complex from the purple photosynthetic bacterium Rhodopseudomonas acidophila strain 10050. Prog Biophys Molec Biol 68 1-27 Connors RE, Burns DS, Farhoosh R and Frank HA (1993) Computational studies of the molecular structure andelectronic spectroscopy of Carotenoids. J Phys Chem 97 9351-9355 De Las Rivas J, Telfer A and Barber J (1993) Two coupled carotene molecules protect P680 from photodamage in isolated Photosystem 11 reaction centres. Biochim Biophys Acta 1142 155-164... [Pg.217]

Cogdell RJ, Isaacs NW, Freer AA, Arrelano J, Howard TD, Papiz MZ, Hawthomthwaite-Lawless AM and Prince SM. The structure and function of the LH2 (B800-850) complex from the purple photosynthetic bacterium Rhodopseudomonas acidophila strain 10050. Prog. Biophys. Molec. Biol. 1997 68 1-27. [Pg.88]

Proteobacteria (Imhoff, 1995). The functions of carotenoids in photosynthetic bacteria have been investigated in most detail in the Rhodospirillaceae (other chapters in this book). Their RC resembles that of PS 11 of green plants. Their major BChl is BChl a or b. The RC was firstly crystallized from Bla. (previously, Rhodopseudomonas) viridis, and the localization of one carotenoid, 1,2-dihydroneuro-sporene, four BChl b and two bacteriopheophytin b molecules was determined (Deisenhofer et al., 1995). A similar localization of spheroidene in the RC of Rba. sphaeroides has also been described (Yeates et al., 1988 Ermler et al., 1994). The fine crystal structure of the LH II antenna complex from Rps. acidophila strain 10050 has shown the localization of one rhodopin glucoside and three BChl a molecules per ap monomer (McDermott et al., 1995). A similar localization of lycopene in the LH II complex from Rsp. molischiamm has also described (Koepke et al,... [Pg.58]

Pure Appl Chem69 2163-2168 Schmidt K (1971) Carotenoids of purple nonsulfur bacteria Composition and biosynthesis of the carotenoids of some strains of Rhodopseudomonas acidophila, Rhodospirillum tenue, and Rhodocyclus purpureus. Arch Mikrobiol 77 231-238... [Pg.68]

See other pages where Rhodopseudomonas acidophila strain is mentioned: [Pg.92]    [Pg.296]    [Pg.92]    [Pg.296]    [Pg.151]   
See also in sourсe #XX -- [ Pg.71 , Pg.74 ]



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Rhodopseudomonas acidophila

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