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Rhodopseudomonas viridis spectroscopy

Thompson MA, Zemer MC (1991) A theoretical examination of the electronic structure and spectroscopy of the photosynthetic reaction center from Rhodopseudomonas viridis. J Am Chem Soc 113 8210-8215... [Pg.328]

Breton, J., Bibikova, M., Oesterhelt, D., and Nabedryk, E., 1999, Conformational heterogeneity of the bacteriopheophytin electron acceptor in reaction centers from Rhodopseudomonas viridis revealed by Fourier transform infrared spectroscopy and site-directed mutagenesis. Biochemistry, 38 11541nll552. [Pg.667]

Zinth, W., and Kaiser, W., 1993, Time-resolved spectroscopy of the primary electron transfer in reaction centers of Rhodobacter sphaeroides and Rhodopseudomonas viridis. In The Photosynthetic Reaction Center, (J. Deisenhofer and J. R. Norris, eds.) Volume 2, 71988, Academic Press, San Diego, USA. [Pg.676]

Fig. 9. (A) Absorption spectrum of Rb. sphaeroides used as a reference to show the Qx and Qy bands of the primary donor (P), BChl [B] and bacteriopheophytin [BO] (B) Femtosecond absorption changes at 920 (a), 785 (b) and 545 nm (c) vs. the delay time of the monitoring pulse measured at room temperature, and (C) absorption changes at 920 (a) and 794 nm (b) measured at 25 K. Figure source (A) see Fig. 7 (B) Holzapfel, Finkele, Kaiser, Oesterheldt, Scheer, Stilz and Zinth (1990) Initial electron transferin the reaction center from Rhodobacter sphaeroides. Proc Nat Acad Sci, USA 87 5170 (C) Zinth and Kaiser (1993) Time-resolved spectroscopy of the primary electron transfer in reaction centers of Rhodobacter sphaeroides and Rhodopseudomonas viridis. I n JR Norris and J Deisenhofer (eds) The Photosynthetic Reaction Center, Voi il, p 82. Acad Press. Fig. 9. (A) Absorption spectrum of Rb. sphaeroides used as a reference to show the Qx and Qy bands of the primary donor (P), BChl [B] and bacteriopheophytin [BO] (B) Femtosecond absorption changes at 920 (a), 785 (b) and 545 nm (c) vs. the delay time of the monitoring pulse measured at room temperature, and (C) absorption changes at 920 (a) and 794 nm (b) measured at 25 K. Figure source (A) see Fig. 7 (B) Holzapfel, Finkele, Kaiser, Oesterheldt, Scheer, Stilz and Zinth (1990) Initial electron transferin the reaction center from Rhodobacter sphaeroides. Proc Nat Acad Sci, USA 87 5170 (C) Zinth and Kaiser (1993) Time-resolved spectroscopy of the primary electron transfer in reaction centers of Rhodobacter sphaeroides and Rhodopseudomonas viridis. I n JR Norris and J Deisenhofer (eds) The Photosynthetic Reaction Center, Voi il, p 82. Acad Press.
J Breton, J-L Martin, A Migus, A Antonetti and A Orszag (1986) Femtosecond spectroscopy of excitation energy transfer and initial charge separation in the reaction center of the photosynthetic bacterium Rhodopseudomonas viridis. Proc Nat Acad Sci, USA 83 5121-5125... [Pg.146]

Table 1. Summary of experimental data obtained by EPR spectroscopy on g, kinetics of photooxidation of the four cytochromes in Rp. viridis. Data from Nitschke and Rutherfored (1989) Tetraheme cytochrome c subunit of Rhodopseudomonas viridis bv EPR. Biochemistry 28 3161-3168. Table 1. Summary of experimental data obtained by EPR spectroscopy on g, kinetics of photooxidation of the four cytochromes in Rp. viridis. Data from Nitschke and Rutherfored (1989) Tetraheme cytochrome c subunit of Rhodopseudomonas viridis bv EPR. Biochemistry 28 3161-3168.
Rhodopseudomonas viridis by genetic analysis, electron paramagnetic resonance and optical spectroscopy. Biochemistry 28 5544-5553... [Pg.121]

D.J. Lockhart and S.G. Boxer, Stark effect spectroscopy of Rhodobacter sphaeroides and Rhodopseudomonas viridis reaction centers, Proc. Natl. Acad. Sci. USA 85 107 (1988). [Pg.604]

Investigation of Quinone Reduction in Rhodopseudomonas viridis by FTIR Difference Spectroscopy and X-Ray Diffraction Analysis... [Pg.75]

Recently we improved the reaction center isolation procedure - A purified preparation still containing the H subunit, and displaying a stable photochemical activity, was obtained - In this article we will compare some functional properties of this reaction center preparation with reference to Rhodopseudomonas viridis and Rhodobacter sphaeroides. Similarities are found with the former at the level of the acceptor quinone complex the structure of the primary donor in both the reduced and oxidized states, as determined by Fourier transform resonance Raman spectroscopy, resembles the latter. [Pg.133]


See other pages where Rhodopseudomonas viridis spectroscopy is mentioned: [Pg.77]    [Pg.1122]    [Pg.134]    [Pg.109]    [Pg.20]    [Pg.135]   
See also in sourсe #XX -- [ Pg.26 , Pg.27 , Pg.28 , Pg.29 ]




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Rhodopseudomonas viridis

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