Rhodopseudomonas viridis photosynthetic reaction center

Scherer, P. O. J., and Fischer, S. F., 1989, Long-range elecfton-ftansfer within the hexamer of the photosynthetic reaction center Rhodopseudomonas viridis. J. Phys. Chem., 93 1633nl637. 

Deisenhofer, J., Michael, H. Nobel lecture. The photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis. EMBO f. 8 2149-2169, 1989. 

Deisenhofer, J., et al. Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 A resolution. Nature 318 618-624, 1985. 

Michel, H. Three-dimensional crystals of a membrane protein complex. The photosynthetic reaction center from Rhodopseudomonas viridis.. Mol. Biol. 

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. 

What molecular architecture couples the absorption of light energy to rapid electron-transfer events, in turn coupling these e transfers to proton translocations so that ATP synthesis is possible Part of the answer to this question lies in the membrane-associated nature of the photosystems. Membrane proteins have been difficult to study due to their insolubility in the usual aqueous solvents employed in protein biochemistry. A major breakthrough occurred in 1984 when Johann Deisenhofer, Hartmut Michel, and Robert Huber reported the first X-ray crystallographic analysis of a membrane protein. To the great benefit of photosynthesis research, this protein was the reaction center from the photosynthetic purple bacterium Rhodopseudomonas viridis. This research earned these three scientists the 1984 Nobel Prize in chemistry. 

It is interesting to compare the thermal-treatment effect on the secondary structure of two proteins, namely, bacteriorhodopsin (BR) and photosynthetic reaction centers from Rhodopseudomonas viridis (RC). The investigation was done for three types of samples for each object-solution, LB film, and self-assembled film. Both proteins are membrane ones and are objects of numerous studies, for they play a key role in photosynthesis, providing a light-induced charge transfer through membranes—electrons in the case of RC and protons in the case of BR. 

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... 

Figure 6.2. (a) Photosynthetic reaction center of Rhodopseudomonas viridis Reprinted from the Protein Data Bank, H. M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T. N. Bhat, H. Weissig, I. N. Shindyalov, P. E. Bourne, Nucleic Acids Res. 2000, 1, 235 (http // www.pdb.org/) PDB ID IDXR, C. R. D. Lancaster, M. Bibikova, P. Sabatino, D. Oesterhelt, H. Michel, J. Biol Chem. 2000, 275, 39364. (b) arrangement of the essential components in the purple bacterium Rh. sphaeroides. [Adapted from Ref. 5.]... 

Figure 23-31 (A) Stereoscopic ribbon drawing of the photosynthetic reaction center proteins of Rhodopseudomonas viridis. Bound chromophores are drawn as wire models. The H subunit is at the bottom the L and M subunits are in the center. The upper globule is the cytochrome c. The view is toward the flat side of the L, M module with the L subunit toward the observer. (B) Stereo view of only the bound chromophores. The four heme groups Hel-He4, the bacteriochlorophylls (Bchl) and bacteriopheophytins (BPh), the quinones QA and QB/ and iron (Fe) are shown. The four hemes of the cytochrome are not shown in...

J. Hasegawa and H. Nakatsuji, Mechanism and unidirectionality of the electron transfer in the photosynthetic reaction center of Rhodopseudomonas Viridis SAC-CI theoretical study, J. Phys. Chem. B, 102 (1998) 10420-10430. 

Thomson, M.A. and Schenter G.K., Excited States of the Bacteriochlorophyll b Dimer of Rhodopseudomonas viridis A QM/MM Study of the Photosynthetic Reaction Center That Includes MM Polarization. J. Phys. Chem. (1995) 99 6374-386. 

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...

See, e.g., J. Deisenhofer, H. Michel, The Photosynthetic Reaction Center from the Purple Bacterium Rhodopseudomonas-Viridis. Science 1989, 245, 1463-1473 M. E. Michel-Beyerle, M. Plato, J. Deisenhofer, H. Michel, M. Bixton, J. Jortner, Unidirectionality of Charge Separation in Reaction Centers of Photosynthetic Bacteria. Biochim. Biophys. Acta 1988, 932, 52-70. 

Meyer, T. E., Bartsch, R. G., Cusanovich, M. A., and Tollin, G., 1993, Kinetics of photooxidation of soluble cytochromes, hipip, and azurin by the photosynthetic reaction center of the purple phototrophic bacterium Rhodopseudomonas viridis Biochemistry 32 471994726. 

Michel, H., Deisenhofer, J., and Epp, O., 1986, Pigment protein interactions in the photosynthetic reaction center from Rhodopseudomonas viridis Embo J. 5 244592451. 

Sinning, I., Koepke, J., Schiller, B., and Michel, H., 1990, 1st glance on the 3-dimensional structure of the photosynthetic reaction center from a herbicide-resistant Rhodopseudomonas viridis mutant. Zeitschrift fur Naturforschung C, 45 455fi458. 

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. 

Deisenhofer, J., Epp, O., Miki, K., Huber, R., Michel, H. (1984) X-ray Structure Analysis of a Membrane Protein Complex. Electron Density Map at 3 A Resolution and a Model of the Chromo-phores of the Photosynthetic Reaction Center from Rhodopseudomonas viridis, J. Mol. Biol. 180, 385-398. 

M.A. Thompson and G.K. Schenter, Excited states of the bacteriochloro-phyll b dimer of Rhodopseudomonas viridis A QM/MM study of the photosynthetic reaction center that includes MM polarization, J. Phys. Chem., 99 (1995), 6374-6386. 

A crucial protein at the photosynthetic reaction center of the purple bacterium Rhodopseudomonas viridis (see Section 20.6) has been separated from the organism, crystallized, and studied by x-ray diffraction. This substance crystallizes with a primitive unit cell in the tetragonal sys-... 

Fig. 9. Stereo view of the three-dimensional arrangement of the pigment moiecules and cofactors in the Rp. viridis reaction center without the background protein structures. He=heme. Figure constructed as a composite from Deisenhofer, Michel and Huber (1985) The structural basis of photosynthetic light reactions in bacteria. Trends Biochem Sci, 10 245 and Deisenhofer and Michel (1993) Three-dimensional structure of the reaction center of Rhodopseudomonas viridis. In J Deisenhofer and JR Norris (eds) The Photosynthetic Reaction Center, Vol. II, p 348. 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.

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