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Membranes thylakoid

Traditionally, the electron and proton transport pathways of photosynthetic membranes (33) have been represented as a "Z" rotated 90° to the left with noncycHc electron flow from left to right and PSII on the left-most and PSI on the right-most vertical in that orientation (25,34). Other orientations and more complex graphical representations have been used to depict electron transport (29) or the sequence and redox midpoint potentials of the electron carriers. As elucidation of photosynthetic membrane architecture and electron pathways has progressed, PSI has come to be placed on the left as the "Z" convention is being abandoned. Figure 1 describes the orientation in the thylakoid membrane of the components of PSI and PSII with noncycHc electron flow from right to left. [Pg.39]

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,... [Pg.40]

The PSII complex contains two distinct plastoquiaones that act ia series. The first is the mentioned above the second, Qg, is reversibly associated with a 30—34 kDa polypeptide ia the PSII cote. This secondary quiaone acceptor polypeptide is the most rapidly tumed-over proteia ia thylakoid membranes (41,46). It serves as a two-electron gate and connects the single-electron transfer events of the reaction center with the pool of free... [Pg.42]

Plant cells contain a unique family of organelles, the plastids, of which the chloroplast is the prominent example. Chloroplasts have a double membrane envelope, an inner volume called the stroma, and an internal membrane system rich in thylakoid membranes, which enclose a third compartment, the thylakoid lumen. Chloroplasts are significantly larger than mitochondria. Other plastids are found in specialized structures such as fruits, flower petals, and roots and have specialized roles. [Pg.29]

Chloroplasts are the site of photosynthesis, the reactions by which light energy is converted to metabolically useful chemical energy in the form of ATP. These reactions occur on the thylakoid membranes. The formation of carbohydrate from CO9 takes place in the stroma. Oxygen is evolved during photosynthesis. Chloroplasts are the primary source of energy in the light. [Pg.29]

Characteristic of all chloroplasts, however, is the organization of the inner membrane system, the so-called thylakoid membrane. The thylakoid membrane... [Pg.710]

FIGURE 22.4 The light-dependent and light-independent reactions of photosynthesis. Light reactions are associated with the thylakoid membranes, and light-independent reactions are associated with the stroma. [Pg.712]

Detergent treatment of a suspension of thylakoids dissolves the membranes, releasing complexes containing both chlorophyll and protein. These chlorophyll-protein complexes represent integral components of the thylakoid membrane, and their organization reflects their roles as either light-harvesting com-... [Pg.717]

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.)... [Pg.726]

The thylakoid membrane is asymmetrically organized, or sided, like the mitochondrial membrane. It also shares the property of being a barrier to the passive diffusion of H ions. Photosynthetic electron transport thus establishes an electrochemical gradient, or proton-motive force, across the thylakoid membrane with the interior, or lumen, side accumulating H ions relative to the stroma of the chloroplast. Like oxidative phosphorylation, the mechanism of photophosphorylation is chemiosmotic. [Pg.727]

FIGURE 22.21 The mechanism of photophosphorylation. Photosynthetic electron transport establishes a proton gradient that is tapped by the CFiCFo ATP synthase to drive ATP synthesis. Critical to this mechanism is the fact that the membrane-bound components of light-induced electron transport and ATP synthesis are asymmetrical with respect to the thylakoid membrane so that vectorial discharge and uptake of ensue, generating the proton-motive force. [Pg.729]

When light-driven proton pumping across the thylakoid membrane occurs, a concomitant efflux of Mg ions from vesicles into the stroma is observed. This efflux of Mg somewhat counteracts the charge accumulation due to H ... [Pg.736]

Cramer, W. A., et al., 1985. Topogi aphy and function of thylakoid membrane proteins. Trends in Biochemical Sciences 10 125-129. [Pg.741]

Anderson, J.M. (1986). Photoregulation of the composition, function, and structure of thylakoid membranes. Annual Review of Plant Physiology, 37, 93-136. [Pg.63]

Some plant HSPs are known to be associated with chloroplasts. Although chloroplasts and mitochondria do not synthesise HSP themselves (Nieto-Sotelo Ho, 1987), certain nuclear encoded HSPs synthesised in the cytosol have been shown to be transported into chloroplasts (Kloppstech et al., 1985 Vierling et al., 1986). The HSP22 of Chlamydomonas is incorporated into the thylakoid membrane without size reduction, while in pea, HSP22 is synthesised as a 26 kDa precursor. In Chlamydomonas, Schuster et al. (1988) have shown that the HSP22 is associated with the photosystem... [Pg.162]

The carotenoids are located in photosynthetic pigment-protein complexes (PPCs) in the thylakoid membranes (Young, 1993), with minor amounts in the chloroplast envelope (Joyard et al, 1991) and the envelope of amyloplasts (Fishwick and Wright, 1980). In all plastid envelope membranes, violaxanthin is the major carotenoid. Carotenes are also found in plastoglobuli (Lichtenthaler and Peveling, 1966). [Pg.255]

The chlorophyU-protein complexes located in the hydrophobic thylakoid membrane are accompaified by xanthophyUs, certain carotenes, and tocopherols (depend-... [Pg.41]

The phycobiliproteins are accessory photosynthetic pigments aggregated in cells as phycobilisomes that are attached to the thylakoid membrane of the chloroplast. The red phycobiliproteins (phycoerythrin) and the blue phycobiliprotein (phycocy-anin) are soluble in water and can serve as natural colorants in foods, cosmetics, and pharmaceuticals. Chemically, the phycobiliproteins are built from chro-mophores — bilins — that are open-chain tetrapyrroles covalently linked via thio-ether bonds to an apoprotein. ... [Pg.411]

Ligeza A, Tikhonov AN, Hyde JS, Subczynski WK. 1998. Oxygen permeability of thylakoid membranes Electron paramagnetic resonance spin labeling study. Biochim Biophys Acta 1365 453. [Pg.690]

Gruszecki, W.I. and K. Strzalka. 1991. Does the xanthophyll cycle take part in the regulation of fluidity of the thylakoid membrane. Biochim. Biophys. Acta 1060 310-314. [Pg.28]

Havaux, M. and W.I. Gruszecki. 1993. Heat- and light-induced chlorophyll a fluorescence changes in potato leaves containing high or low levels of the carotenoid zeaxanthin Indications of a regulatory effect of zeaxanthin on thylakoid membrane fluidity. Photochem. Photobiol. 58 607-614. [Pg.28]

Strzalka, K. and W.I. Gruszecki. 1997. Modulation of thylakoid membrane fluidity by exogenously added carotenoids. J. Biochem. Mol. Biol. Biophys. 1 103-108. [Pg.29]


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