Light energy conversion and water-oxidation systems in photosynthesis

Light energy conversion and water-oxidation systems in photosynthesis 

The main outcome of photosynthesis is the oxidation of water and the synthesis of glucose from carbon dioxide at the expense of sunlight energy. The immensity of this process on the scale of the Earth is evident by the fact that annually about 50 billion tons of carbon from carbon dioxide is bound into forms that provide energy and structural material for all living organisms on Earth (Dismukes, 2001 Blankenship, 2001 Rutherford and Faller, 2001 Witt, 1996). 

The primary photochemical processes of photosynthesis take place within membrane bound complexes of pigments and protein, reaction centers (Shuvalov and Krasnovsky, 1981 Deisenhofer et al., 1986, Rees et al., 1989 Norris and Shiffer, 1990 Kirmaier and Holten, 1991 Feher et al, 1992 Stowell et al, 1997). One mole of a reaction center from different bacteria contains 4 moles of bacteriochlorophyl (Bchl), 2 moles of bacteriopheophytin (Bph), two moles of ubiquinone (Q) and a non-heme Fe atom. In RC from Rhodobacter speroides, a total of 11 hydrophobic a-helixes create a framework that organizes the cofactor and a hydrophobic band approximately 35 A wide. RC from Rhodopseudomonus viridus has three polypeptides having pronounced hydrophobic properties. The molecular mass of the polypeptides are 37 571 (L), 35902 (M) and 28902 (H). The H subunit does not carry pigments but it is sufficient for the photochemical activity. The protein components of reaction centers from different-bacteria are similar. 

The tunneling hypothesis has been supported in subsequent experiments. By the electron paramagnetic resonance measurements (Kulikov et al 1979) the distances 

The first experimental evidences that electron transfer from QA to P+ and from QA to Qb in reaction centers are controlled by the protein conformational dynamics, was obtained in the late 1970 s (Berg 1978a,b Likhtenshtein et al., 1979 a, b) This conclusion was confirmed in subsequent experimental studies in which molecular dynamics of RC and the photsynthetic membrane were determined with a whole set of physical labels. (Kotelnikov et al., 1983, Kochetkov et al., 1984 Parak et al., 1983). It was shown that the electron transfer from reduced primary acceptor QA to secondary acceptor Qb takes place only under conditions in which the labels record the mobility of the protein moiety in the membrane with the correlation frequency u0 107 s-1 (Fig. 3.16). 

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