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Rhodopseudomonas viridis reaction center calculated

Fig. 2. Absorption spectra of BChl a in petroleum ether and the Rb. sphaeroides R-26 reaction-center preparation (A) and of BChl b in ether and in the BChl b-containing Rhodopseudomonas viridis reaction-center preparation (B). Figure source (A) Reed and Peters (1972) Characterization of the pigments in reaction center preparation from Rhodopseudomonas sphaeroides. J Biol Chem 246 7148 (B) Parson, Scherz and Warshel (1985) Calculation of spectroscopic properties of bacterial reaction centers. In ME Michel-Bayerle (ed) Antennas and Reaction Centers of Photosynthetic Bacteria, p 123. Springer Verlag. Fig. 2. Absorption spectra of BChl a in petroleum ether and the Rb. sphaeroides R-26 reaction-center preparation (A) and of BChl b in ether and in the BChl b-containing Rhodopseudomonas viridis reaction-center preparation (B). Figure source (A) Reed and Peters (1972) Characterization of the pigments in reaction center preparation from Rhodopseudomonas sphaeroides. J Biol Chem 246 7148 (B) Parson, Scherz and Warshel (1985) Calculation of spectroscopic properties of bacterial reaction centers. In ME Michel-Bayerle (ed) Antennas and Reaction Centers of Photosynthetic Bacteria, p 123. Springer Verlag.
The photosynthetic reaction center is currently the only membrane protein complex whose structure is known to atomic resolution [15]. Before the three-dimensional structure was actually solved by X-ray diffraction, however, protein hydropathy plots were used to show the existence of a total of 11 transmembrane helices in the three subunits H, L and M by analyzing the deduced amino acid sequence of the reaction center genes [16]. Figure 2 shows the hydropathy plots of the L and M subunits of the Rhodopseudomonas viridis reaction center using a window of 19 residues. The upper trace within each panel is obtained from the semi-empirical amino acid residue hydropathy values [11], and the lower trace is calculated using the nucleotide-determined values from SVD (without translation). Although the plots do not take codon usage or the NGN problem into account, each pair is nevertheless virtually identical (the protein hydropathy has been displaced for display purposes). The A, B, C, D, and E transmembrane helices of each subunit are easily identified as relative maxima. [Pg.213]

Figure 4-7. Electronic factors in the rate constant calculated for the electron transfers in the bacterial photosynthetic reaction centers of (a) Rhodopseudomonas viridis, and (b) Rhodobactor sphaeroides... Figure 4-7. Electronic factors in the rate constant calculated for the electron transfers in the bacterial photosynthetic reaction centers of (a) Rhodopseudomonas viridis, and (b) Rhodobactor sphaeroides...
Lancaster CRD, ErmlerU and Michel H (1995) The structures of photosynthetic reaction centers from purple bacteria as revealed by X-ray crystallography. In Blankenship RE, Madigan MT and Bauer CE (eds) Anoxygenic Photosynthetic Bacteria, pp 503-526. Kluwer Academic Publishers, Dordrecht Lancaster CRD, Michel H, Honig B and Gunner MR (1996) Calculated coupling of electron and proton transfer in the photosyntheticreaction centre of Rhodopseudomonas viridis. Biophys 1 70 2469-2492... [Pg.121]


See other pages where Rhodopseudomonas viridis reaction center calculated is mentioned: [Pg.403]    [Pg.1122]    [Pg.434]    [Pg.133]    [Pg.239]    [Pg.435]   


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