Photosynthetic Reaction Center of Rhodobacter sphaeroides

Van Brederode, M. E., Jones, M. R., and Van Grondelle, R., 1997a, Fluorescence excitation spech a of membrane bound photosynthetic reaction centers of Rhodobacter sphaeroides in which tyrosine M210 is replaced by byptophan evidence for a new pathway of charge separation. Chem. Phys. Letts., 268 143nl49. 

P. Beroza, D. R. Fredkin, M. Y. Okamura, and G. Feher, Proc. Natl. Acad. Sci. U.S.A., 88, 5804 (1991). Protonation of Interacting Residues in a Protein by a Monte Carlo Method Application to Lysozyme and the Photosynthetic Reaction Center of Rhodobacter sphaeroides. 

Walden, S. E. Wheeler, R. A. "Protein Conformational Gate Controlling Binding Site Preference and Migration of Ubiquinone-B in the Photosynthetic Reaction Center of Rhodobacter sphaeroides,"J. Phys. Chem. B 2002, 106, 3001-3006. 

Jonas D M, Lang M J, Nagasawa Y, Joo T and Fleming G R 1996 Pump-probe polarization anisotropy study of femtosecond energy transfer within the photosynthetic reaction-center of Rhodobacter sphaeroides R26 J. Phys. 

Beroza, R, Fredkin, D.R., Okamura, M.Y., Feher, G. Protonation of interacting residues in a protein by a Monte Carlo method Application to lysozyme and the photosynthetic reaction center of Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. USA 1991, 88, 5804-8. 

Fig. 6.7 FTIR difference spectrum (light-minus-dark) of the absorbance changes associated with electron transfer from the special pair of bacteriochlorophylls (P) to a quinone (Qa) in photosynthetic reaction centers of Rhodobacter sphaeroides. The negative absorption changes result mainly from loss of absorption bands of P the positive changes, from the absorption bands of the oxidized dimer (P ). These measurements were made with a thin film of reaction centers at 100 K. The amplitudes are scaled arbitrarily. Adapted from [101]...

Site-Directed Mutagenesis of Threonine M222 and Tryptophan M252 in the Photosynthetic Reaction Center of Rhodobacter sphaeroides... 

Table 12.2 Amino acid sequences of the transmembrane helices of the photosynthetic reaction center in Rhodobacter sphaeroides...

Photosynthetic reaction centers from Rhodobacter sphaeroides and bacteri-orhodopsin (BR) from purple membrane (PM) have been used for their unique optoelectronic properties and for their capability of providing light-induced proton and electron pumping. Once assembled they display extremely high thermal and temporal stability... 

Ishikita, H. Morra, G. Knapp, E.W., Redox potential of quinones in photosynthetic reaction centers from Rhodobacter sphaeroides dependence on protonation of Glu-L212 and Asp-L213, Biochemistry 2003, 42, 3882-3892... 

Beroza, P., Fredkin, D. R., Okamura, M. Y., and Feher, G., 1992, Proton transfer pathways in the reaction center of Rhodobacter sphaeroides a computational study. In The Photosynthetic Bacterial Reaction Center II (J. Breton and A. VermEglio, eds.) pp. 3639374. Plenum Press, New York. 

Chang, C. H., El Kabbani, O., Tiede, D., Norris, J., and Schiffer, M., 1991, Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry, 30 5352115360. 

Chirino, A. J., Lous, E. J., Huber, M., Allen, J. P., Schenck, C. C., Paddock, M. L., Feher, G., and Rees, D. C., 1994, Crystallographic analyses of site-directed mutants of the photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry, 33 458494593. 

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. 

Figure 14 Structure of the photosynthetic reaction center from Rhodobacter sphaeroides in the region of the Fe + and quinones. The residue numbers refer to the L and M subunits of the reaction center...

Figure 4 Proton transfer pathway in the photosynthetic reaction center from Rhodobacter sphaeroides connects the soivent-exposed part of the protein (Hisl 26-Hisl 28) to the secondary quinone binding site Qg (6).

Fig. 8. Three-dimensional structure of the photosynthetic reaction center of Rb. sphaeroides R-26. The a-helices are drawn as columns. Modified from the original color drawing of Allen, Feher, Yeates, Komiya and Rees (1987) Structure of the reaction center from Rhodobacter sphaeroides R-2. The protein subunits. Proc Nat Acad Sci, USA, 84 6165.

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.

C Lautwasser, U Finkele, H Scheer and WZinth (1991) Temperature dependence of the primary electron transfers photosynthetic reaction centers from Rhodobacter sphaeroides. Chem Phys Lett 183 471-477... 

Stilz HU, Finkele U, Holzapfel W, Lauterwasser C, Zinth W and Oesterhelt D (1994) Influence ofM subunit Thr222 and Trp252 on quinone binding and electron transfer in Rhodobacter sphaeroides reaction centres. Eur J Biochem 223 233-242 Stowell MHB, McPhillips TM, Rees DC, Soltis SM, Abresch E and Feher G (1997) Light-induced structural changes in photosynthetic reaction center Implications for mechanism of electron-proton transfer. Science 276 812-816 Takahashi E and Wraight CA (1996) Potentiation of proton transfer function by electrostatic interactions in photosynthetic reaction centers from Rhodobacter sphaeroides First results... 

Tiede DM, Budil DE, Tang J et al. Symmetry breaking structures involved in the docking of cytochrome c and primary electron transfer in reaction centers of rhodobacter sphaeroides. In Breton J, Vermeglio A, eds. The Photosynthetic Bacterial Reaction Center, Structure and Dynamics. New York Plenum, 1988 13-20. 

Agostiano A, Caselli M, Cosma P et al. Electrochemical investi tion of the intercation of different mediators with the photosynthetic reaction center from rhodobacter sphaeroides. Electrochim Acta... 

The arrangement of the two reaction center proteins D1 and D2, was based on studies of its stmctural and functional analogues, L and M subunits of the reaction centers of Rhodobacter sphaeroides and Rhodopseudomonas viridis The D1 protein is membrane protein which contains five trans-membranes helices (A-E) and two short parallel helices that do not span the membrane. One of them, the DE helix is located between the fourth and fifth D and E) transmembrane regions. It was exposed to the stromal side (the acceptor side) of the photosynthetic membrane. It was found that this region of the DI protein formed the binding niche of the secondary quinone (Qb). There were a number of D2 protein residues that were also identified as part of the Qp-niche. ... 

Fig. 2. (A) Absorption spectra of photosynthetic reaction centers from Rhodobacter sphaeroides at low (solid line) and high light intensity (dashed line). All spectra were recorded with an integration time of 5 msec. (B) Time course of the bleaching under the lowest useful conditions. Compare the time scale to typical HPLC conditions at a flow rate of 1.5 ml/ min, and 8 /xl cell volume, the sample spends 330 msec in the cell of the detector.

Utschig LM, Thumauner MC, Tiede DM, Poluektov OG. 2005. Low-temperature in-terquinone electron transfer in photosynthetic reaction centers from Rhodobacter sphaeroides and Blastochloris viridis characterization of Q(B)(-) states by high-... 

Calvo R, Ahresch EC, Bittl R, Feher G, Hofbauer W, Isaacson RA, Luhitz W, Okamura MY, Paddock ML. 2000. EPR study of the molecular and electronic structure of the semiquinone hiradical Qa Qb hi photosynthetic reaction centers from Rhodobacter sphaeroides. J Am Chem Soc 122(30) 7327-7341. 

Tryptophan M252 is located between the bacteriopheophytin and the quinone in the photosynthetic reaction center of Rhodobacter (Rb.) sphaeroides (1-4). The indole ring of the tryptophan M252 is in van der Waals contact with both the bacteriopheophytin and the quinone and was suspected from this unique position to participate as a (superexchange) mediator in electron transfer (5). At the same time tryptophan M252 may contribute via a charge transfer interaction to the binding of quinone to the Qj site (6). ... 

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