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Pigment, photosynthetic

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 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 12.14 The three-dimensional structure of a photosynthetic reaction center of a purple bacterium was the first high-resolution structure to be obtained from a membrane-bound protein. The molecule contains four subunits L, M, H, and a cytochrome. Subunits L and M bind the photosynthetic pigments, and the cytochrome binds four heme groups. The L (yellow) and the M (red) subunits each have five transmembrane a helices A-E. The H subunit (green) has one such transmembrane helix, AH, and the cytochrome (blue) has none. Approximate membrane boundaries are shown. The photosynthetic pigments and the heme groups appear in black. (Adapted from L. Stryer, Biochemistry, 3rd ed. New York ... Figure 12.14 The three-dimensional structure of a photosynthetic reaction center of a purple bacterium was the first high-resolution structure to be obtained from a membrane-bound protein. The molecule contains four subunits L, M, H, and a cytochrome. Subunits L and M bind the photosynthetic pigments, and the cytochrome binds four heme groups. The L (yellow) and the M (red) subunits each have five transmembrane a helices A-E. The H subunit (green) has one such transmembrane helix, AH, and the cytochrome (blue) has none. Approximate membrane boundaries are shown. The photosynthetic pigments and the heme groups appear in black. (Adapted from L. Stryer, Biochemistry, 3rd ed. New York ...
The structurally similar L and M subunits are related by a pseudo-twofold symmetry axis through the core, between the helices of the four-helix bundle motif. The photosynthetic pigments are bound to these subunits, most of them to the transmembrane helices, and they are also related by the same twofold symmetry axis (Figure 12.15). The pigments are arranged so that they form two possible pathways for electron transfer across the membrane, one on each side of the symmetry axis. [Pg.237]

Figure 12.15 Schematic arrangement of the photosynthetic pigments in the reaction center of Rhodopseudomonas viridis. The twofold symmetry axis that relates the L and the M subunits is aligned vertically in the plane of the paper. Electron transfer proceeds preferentially along the branch to the right. The periplasmic side of the membrane is near the top, and the cytoplasmic side is near the bottom of the structure. (From B. Furugren, courtesy of the Royal Swedish Academy of Science.)... Figure 12.15 Schematic arrangement of the photosynthetic pigments in the reaction center of Rhodopseudomonas viridis. The twofold symmetry axis that relates the L and the M subunits is aligned vertically in the plane of the paper. Electron transfer proceeds preferentially along the branch to the right. The periplasmic side of the membrane is near the top, and the cytoplasmic side is near the bottom of the structure. (From B. Furugren, courtesy of the Royal Swedish Academy of Science.)...
The helices are aligned according to approximate positions within the membrane and with respect to the photosynthetic pigments. LA is the first helix of subunit L, ME is the last helix of subunit M, HA is the only transmembrane helix of subunit H. Charged residues are eol-ored red, polar residues are blue, hydrophobic residues are green, and glycine is yellow. (From T.O. Yeates et al., Proc. Natl. Acad. Sci. USA 84 6438-6442, 1987.)... [Pg.247]

The Fate of Light Energy Absorbed by Photosynthetic Pigments... [Pg.714]

Each photon represents a quantum of light energy. A quantum of light energy absorbed by a photosynthetic pigment has four possible fates (Figure 22.8) ... [Pg.714]

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 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]

Such a process can naturally be expected to play a certain part in the mechanism of directed energy transport in biological systems, in particular, in the transfer of absorbed energy from the antenna chlorophyll molecules to the reactive center in the photosynthetic system of plants. In Ref. [30], energy exchange between molecules of the photosynthetic pigments chlorophyll a and pheophytin a was studied experimentally with pigments introduced into the polar matrix. [Pg.199]

Zenkevich RAN, El NNA, Tomin VI (1982) Directed energy transfer due to orientational broadening of energy levels in photosynthetic pigments solutions. J Lumin 26 367-376... [Pg.221]

Maynard Smith, J. and Szathmary, E. (1998). The Origins of Life. Oxford University Press, Oxford. Morowitz, H. (2002). The Emergence of Everything. Oxford University Press Inc., New York. Mulkidjanian, A.Y., and Junge, W. (1999). Primordial UV-protectors as ancestors of the photosynthetic pigment protein. In G. A. Peshek, et al. (eds). The Phototropic Prokaryotes. Kluwer Academic Press Pub., New York, pp. 805-812... [Pg.463]

Renger, T., May, V. and Kuhn, O. (2001). Ultrafast excitation energy dynamics in photosynthetic pigment protein complexes. Phys. Rep. 343, 137-254. [Pg.68]

The isoprenoid hycrocarbons pristane and phytane (derived from the phytol side chain of chlorophyll), as well as porphyrins, have been detected in organic extracts of the Nonesuch Shale of 1.1 billion year age [23]. Their presence points to the existence of photosynthetic pigments in the Precambrian era, but it is also possible that these extractable substances could have been contributed to the rock at a later time. However, in this instance contamination appears to be less likely on account of the large abundance of organic material in this shale. [Pg.393]

Conway, H.L. 1978. Sorption of arsenic and cadmium and their effects on growth, micronutrient utilization, and photosynthetic pigment composition of Asterionella formosa. Jour. Fish. Res. Board Canada 35 286-294. [Pg.71]

M. Miyake, M. Sekine, L. G.. Vasilieva, E. Nakada, T. Wakayama, Y. Asada, J. Miyake (1998) Improvement of bacterial light-dependent hydrogen production by altering the photosynthetic pigment ratio. BioHydrogen, edited by Zaborsky et al. [Pg.54]


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