Electron transfer in photosynthetic reaction centers

Warshel, A. Chu, Z.T. Parson, W.W., Dispersed polaron simulations of electron transfer in photosynthetic reaction centers, Science 1989, 246, 112-116. 

Rapid Electron Transfer in Photosynthetic Reaction Centers... 

Allen, J. P., and Williams, J. C., 1995, Relationship between the oxidation potential of the bacteriochlorophyll dimer and electron transfer in photosynthetic reaction centers. J. Bioenerg. Biomemb., 27 2759283. 

Chan, C. K., Chen, L. X. Q., Di Magno, T. J., Hanson, D. K., Nance, S. L., Schiffer, M., Norris, J. R., and Fleming, G. R., 1991, Initial electron transfer in photosynthetic reaction centers of Rhodobacter capsulatus mutants. Chem. Phys. Letts., 176 366n372. 

Electron Transfer in Photosynthetic Reaction Centers Sethulakshmi Kartha, Ranjan Das, and James A. Norris... 

The key question with regard to the pathway of the primary electron transfer in photosynthetic reaction centers is addressing the role of the monomer bacteriochlorophyll. In the structure of RMridis [1] and Rb,sphaeroides [2] reaction centers (RCs) this bacteriochlorophyll molecule (B) has been shown to be located between the bacteriochlorophyll dimer, acting as the primary donor ( P ), and a bacteriopheophytin (H). If we consider the participation of B through the state (P B ) there are in principle two ways of such an involvement of B ... 

Fleming, G.R., Martin, J.-L., Breton, J. Rates of primary electron transfer in photosynthetic reaction centers and their mechanistie implications. Nature 333, 190-192 (1988)... 

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-... 

C. Lauterwasser, U. Finkele, H. Scheer, and W. Zinth, Temperature dependence of the primary electron transfer in photosynthetic reaction centers from Rhodo hacter sphaeroides, Chem Phys, Lett, 183 471 (1991). 

FEMTOSECOND SPECTROSCOPY OF THE PRIMARY ELECTRON TRANSFER IN PHOTOSYNTHETIC REACTION CENTERS... 

J-L Martin, J Breton, AJ Hoff, A Migus, and A Antonetti (1986) Femtosecond spectroscopy of electron transfer In the reaction center of the photosynthetic bacterium Rhodopseudomonas sphaeroides R-26 Direct electron transfer from the dimeric bacteriochiorophyii primary donor to the bacteriopheophytin acceptor with a time constant of2.8 0.2ps. Proc Nat Acad Sci, USA 83 957-961... 

There are totally 11 chromophores in the bacterial photosynthetic reaction center (PSRC) of Rhodopseudomonas (Rps.) virids. Since the excitation process of the reaction center is the primary event of the photo-induced electron transfer in the reaction center, the detailed analysis of the absorption spectrum is one of the key steps for the understanding of photochemistry of the system. The chromophores included in the PSRC are bacteriochlorophyll b dimer (special pair, P), bacteriochlorophyll in L- and M-branches (Bl and B ), bacteriopheophytin in L- and M-branches (Hl and Hm), menaquinone (MQ), ubiquinone (UQ) and four different hemes, c-552, c-554, c-556, and c-559 in c-type cytochrome subunit. 

Kong J, Sun W, Wu X et al. Fast reversible electron transfer for photosynthetic reaction center from wild type Rhodobacter sphaeroides reconstituted in polycation sandwiched monolayer film. Bioelectrochem Bioenerg 1999 48 101-107. 

Figure 40 The charge separation within the iecial pair and successive electron transfers in the reaction center of photosynthetic bacteria. (BChl)2, bacteriochl< -q)hyll dimer, BChl, bacteriochlorophyll monomer QA, QB, ubiquinones [424].

Parson, W.W. and Warshel, A., Simulations of electron transfer in bacterial reaction centers, in The Photosynthetic Reaction Center, VoL II, Deisenhofer, J. and Norris, J.R., Eds., Academic Press, 1993, p. 23. 

The heme groups of the cytochromes as well as many other transition metal centers act as carriers of electrons. For example, cytochrome c may accept an electron from reduced cytochrome Cj and pass it to cytochrome oxidase or cytochrome c peroxidase. The electron moves from one heme group to another over distances as great as 2 nm. Similar electron-transfer reactions between defined redox sites are met in photosynthetic reaction centers (Fig. 23-31), in metalloflavo-proteins (Fig. 15-9), and in mitochondrial membranes. 

To observe ultrafast electron transfer taking place in photosynthetic reaction centers, what are the possible experimental techniques ... 

When the donors and acceptors lack spherical symmetry, there will also be an orientation dependence. In cases such as those to be discussed below, where the donor and acceptor moieties are linked by covalent bonds, there is considerable evidence that in certain situations the electron transfer occurs through the linkage bonds [22]. Although such linkages are not present in photosynthetic reaction centers, it has been proposed that the accessory Bchl or other intervening material may still take part in electron transfer through a superexchange mechanism [8, 26]. The distance dependence of photoinitiated electron transfer has recently been reviewed [13]. 

Moser, C. C. and Dutton, P. L. (1992) Engineering protein structure for electron transfer function in photosynthetic reaction centers. Biochim. Biophys. Acta, 1101, 171-176. 

Peluso, A., Di Donato, M., and Saracino, G.A.A.. (2000) An alternative way of thinking about electron transfer in proteins Proton assisted electron transfer between the primary and the secondary quinones in photosynthetic reaction centers, J. Chem. Phys. 113, 3212-3218. 

Stowell, M.H.B., McPhillips, T.M., Rees, D.C., Solitis, S.M., Abresch, E. and Feher, G. (1997) Light-induced structural changes in photosynthetic reaction center implications for mechanism of electron-proton transfer, Science (Washington, D. C.) 276, 812-816. 

Giangiacomo, K. M., and Dutton, P. L., 1989, In Photosynthetic Reaction Centers, the Free-Energy Difference for Electron-Transfer Between Quinones Bound at the Primary and Secondary Quinone-Binding Sites Governs the Observed Secondary Site Specificity Proc. Natl. Acad. Set U. S. A. 86 2658n2662. 

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