Reaction center plant

Deisenhofer, J. Michel, H. (1991) Structures of bacterial photosynthetic reaction centers. Annu. Rev. Cell Biol. 7, 1-23. Description of the structure of the reaction center of purple bacteria and implications for the function of bacterial and plant reaction centers. 

Although the structures of the plant reaction centers are not yet known in detail, photosystem II reaction centers resemble reaction centers of purple bacteria in several ways. The amino acid sequences of their two major polypeptides are homologous to those of the two polypeptides that hold the pigments in the bacterial reaction center. Also, the reaction centers of photosystem II contain a nonheme iron atom and two molecules of plastoquinone, a quinone that is closely related to ubiquinone (see fig. 15.10), and they contain one or more molecules of pheophytin a and several... 

Primary steps of photoinduced electron transfer have been studied in plant reaction centers (PS-I and PS-II), by flash absorption and EPR. In PS-I two questions wereinvestigated i) the properties of the primary radical pair P-700+, A0 (kinetics of decay nature of A0, presumably a specialized chlorophyll a decay by recombination to populate the P-700 triplet state) and ii) the nature of the secondary acceptor A,. Extraction-reconstitution experiments indicate that A, is very probably a molecule of vitamin K,. 

A similar conclusion was reached by Feiler, Albouy, Pourcet, Mattioli, Lutz and Roberts from reso-nance-Raman studies of active reaction-center complexes of Chlorobium. They further showed a similarity in the binding of this Chl-a isomer in green-bacterial reaction centers to that of the Chl-type acceptor molecules in other bacteria and green-plant reaction centers. Finally, one may note that the identification of BChl 663 as an isomer of Chi a has placed more emphasis on the similarities between the reaction centers of green sulfur bacteria and the green-plant photosystem I, where the primary electron acceptor is Chi a, and the recently discovered heliobacteria, where the primary electron acceptor is an 8 -hydroxy-Chl a. 

How can a better knowledge of plant reaction center be arrived at To what extent can the knowledge acquired on purple bacteria be used to better understand Photosystems I and II What is the mechanism of water oxidation, a key biological process that proves difficult to unravel ... 

Furthermore, for each reaction the reaction center was specified, information was given on whether the reaction is reversible or irreversible, and catabolic or anabolic. Finally, it was specified whether a reaction is part of a general pathway or occurs only in unicellular organisms, in higher plants, or in animals (Figure 10.3-21). 

Electron Transport Between Photosystem I and Photosystem II Inhibitors. The interaction between PSI and PSII reaction centers (Fig. 1) depends on the thermodynamically favored transfer of electrons from low redox potential carriers to carriers of higher redox potential. This process serves to communicate reducing equivalents between the two photosystem complexes. Photosynthetic and respiratory membranes of both eukaryotes and prokaryotes contain stmctures that serve to oxidize low potential quinols while reducing high potential metaHoproteins (40). In plant thylakoid membranes, this complex is usually referred to as the cytochrome b /f complex, or plastoquinolplastocyanin oxidoreductase, which oxidizes plastoquinol reduced in PSII and reduces plastocyanin oxidized in PSI (25,41). Some diphenyl ethers, eg, 2,4-dinitrophenyl 2 -iodo-3 -methyl-4 -nitro-6 -isopropylphenyl ether [69311-70-2] (DNP-INT), and the quinone analogues,... 

Figure 12.13 Photosynthetic pigments are used hy plants and photosynthetic bacteria to capture photons of light and for electron flow from one side of a membrane to the other side. The diagram shows two such pigments that are present in bacterial reaction centers, bacteriochlorophyll (a) and ubiquinone (b). The light-absorbing parts of the molecules are shown in yellow, attached to hydrocarbon "tails" shown in green.

FIGURE 22.20 The molecular architecture of PSI. PsaA and PsaB constitute the reaction center dimer, an integral membrane complex P700 is located at the lumenal side of this dimer. PsaC, which bears Fe-S centers and Fb, and PsaD, the interaction site for ferre-doxin, are on the stromal side of the thylakoid membrane. PsaF, which provides the plasto-cyaiiin interaction site, is on the lumenal side. (Adapted from Golbeck, J. H., 1992. Amiual Review of Plant Physiology and. Plant Molecular Biology 43 293-324.)... 

Glazer, A. N., and Melis, A., 1987. Photochemical reaction centers Structure, organizadon and fnncdon. Annual Review of Plant Physiology 38 11-45. 

Carotenoids protect photosynthetic organisms against potentially harmful photooxidative processes and are essential structural components of the photosynthetic antenna and reaction center complexes. Plant carotenoids play fundamental roles as accessory pigments for photosynthesis, as protection against photooxidation, and... 

Figure 12.2a. Photosynthetic Z-scheme for green plants. Abbreviations not included in the text are PQ, plastiquinone Cyt bse, a form of cytochrome b absorbing at 564 nm FD, ferredoxin FP a flavoprotein. Long vertical arrows indicate steps arising from photoactivation of pigment reaction centers dashed arrows indicate uncertain pathways.0185...

An interesting process of C-C bond formation is represented by the autooxidation of Mercurialis perennis L. plant alkaloid hermidin. The reaction proceeds through the formation of a transient blue anion-radical, which dimerizes with the transfer of the reaction center to give, eventually, chryso-hermidin as a dimeric hexaketone (Wasserman et al. 1993 Scheme 7.59). 

Until a recent x-ray diffraction study (17) provided direct evidence of the arrangement of the pigment species in the reaction center of the photosynthetic bacterium Rhodopseudomonas Viridis, a considerable amount of all evidence pertaining to the internal molecular architecture of plant or bacterial reaction centers was inferred from the results of in vitro spectroscopic experiments and from work on model systems (5, 18, 19). Aside from their use as indirect probes of the structure and function of plant and bacterial reaction centers, model studies have also provided insights into the development of potential biomimetic solar energy conversion systems. In this regard, the work of Netzel and co-workers (20-22) is particularly noteworthy, and in addition, is quite relevant to the material discussed at this conference. 

On the planet Earth, the most important photoreaction occurs in green plants or in green or purple organisms. Their photochemical reaction centers contain a special pair of chlorins (cf. the purple bacterium Rhodobacter sphaeroides. Fig. 6.2). Solar photons cause electron transfer and generate a radical ion pair. Within two picoseconds, the negative charge is transferred to a second chlorin, and from it to a quinone. ... 

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