Abstract
Life on earth is sustained by oxygenic photosynthesis, a process that involves the absorption and utilization of light energy from the sun. The chemical energy released by this endergonic process results in the oxidation of water molecules, the release of oxygen, and the generation of reductant (reduced ferredoxin and NADPH) and high-energy phosphate bond (ATP). This process takes place in the thylakoid membranes of chloroplasts. It requires coordinated interaction between a large number of electron carrier compounds and enzymatic proteins that facilitate the lateral transport of electrons in the thylakoid membrane from H2O molecules to ferredoxin and NADP+ and the transverse transport of H+ from the surrounding stroma to the enclosed space of the thylakoid lumen. The electron-transport components are localized in the thylakoid membrane and catalyze the transfer of electrons laterally in the plane of the membrane from the grana regions, where oxidation of H2O takes place, to the stroma-exposed thylakoid regions, where the reduction of ferredoxin and the generation of ATP take place (Andersson and Anderson, 1980; Anderson and Melis, 1983). Functionally, electron transport occurs from intermediate to intermediate in a sequential manner formulated as the Z-scheme of photosynthesis (Hill and Bendall, 1960). The overall process of electron transport from H2O to NADP+ is strongly endergonic and is realized through the input and utilization of light energy in two distinct steps. The absorption of light and the conversion of excitation energy to chemical energy takes place in photosystem II (PSII) and photosystem I (PSI) in the thylakoid membrane (Duysens et al., 1961). Light energy in PSII facilitates the generation of a strong oxidant capable of oxidizing H2O molecules. Light energy in PSI facilitates the generation of a strong reductant capable of reducing ferredoxin and NADP+.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Literature Cited
Aizawa, K., Shimizu, T., Hiyama, T., Satoh, K., Nakamura, Y., and Fujita, Y. (1992). Changes in composition of membrane proteins accompanying the regulation of PSI/PSII stoichiometry observed with Synechocystis PCC 6803. Photosynthesis Research 32:131–138.
Allen, J. F. (1992). Protein phosphorylation in regulation of photosynthesis. Biochimica et Biophysica Acta 1098:275–335.
Allen, J. F., Bennett, J., Steinback, K. E., and Arntzen, C. J. (1981). Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems. Nature 291:21–25.
Anderson, J. M., and Chow, W. S. (1992). A regulatory feedback mechanism for light acclimation of the photosynthetic apparatus: Are photosystems II and I self-regulatory sensors? In: Argyroudi-Akoyunoglou, J. H., ed. Regulation of Chloroplast Biogenesis. Plenum Press, New York. pp. 475–482.
Anderson, J. M., and Melis, A. (1983). Localization of different photosystems in separate regions of chloroplast membranes. Proceedings of the National Academy of Sciences of the USA 80:745–749.
Anderson, J. M., Brown, J. S., Lam, E., and Malkin, R. (1983). Chlorophyll b: an integral component of photosystem I of higher plant chloroplasts. Photochemistry and Photobiology 38:205–210.
Anderson, J. M., Chow, W. S., Adamson, H., and Melis, A. (1992). Dynamic light acclimation of the photosynthetic apparatus of higher plants. In: Argyroudi-Akoyunoglou, J. H., ed. Regulation of Chloroplast Biogenesis. Plenum Press, New York. pp. 483–490.
Andersson, B., and Anderson, J. M. (1980). Lateral heterogeneity in the distribution of chlorophyll-protein complexes of the thylakoid membranes of spinach chloroplasts. Biochimica et Biophysica Acta 593:427–440.
Aro, E.-M., Kettunen, R., Tyystjärvi, E. (1992). ATP and light regulate D1 protein modification and degradation: role of D1 in photoinhibition. FEBS Letters 297:29–33.
Aro, E.-M., Virgin, I., and Andersson, B. (1993). Photoinhibition of photosystem II. Inactivation, protein damage and turnover. Biochimica et Biophysica Acta 1143:113–134.
Barber, J. (1989). Function and molecular biology of photosystem II. Oxford Surveys of Plant Molecular and Cell Biology 6:115–162.
Baroli, I., and Melis, A. (1996). Photoinhibition and repair in Dunaliella salina acclimated to different growth irradiances. Planta 198:640–646.
Bennett, J. (1991). Protein phosphorylation in green plant chloroplasts. Annual Review of Plant Physiology and Plant Molecular Biology 42:281–311.
Björkman, O., and Demmig, B. (1987). Photon yield of O2 evolution and chlorophyll fluorescence characteristics at 77 K among vascular plants of diverse origins. Planta 170:489–504.
Björkman, O., and Ludlow, M. M. (1972). Characterization of the light climate on the floor of a Queensland rainforest. Carnegie Institution of Washington Yearbook 71:85–94.
Callahan, F. E., Ghirardi, M. L., Sopory, S. K., Mehta, A. M., Edelman, M., Mattoo, A. K. (1990). Anovel metabolic form of the 32 kDa-D1 protein in the grana-localized reaction center of photosystem II. Journal of Biological Chemistry 265:15357–15360.
Chow, W. S., Haehnel, W., and Anderson, J. M. (1987). The composition and function of thylakoid membranes from pea plants grown under white or green light with or without far-red light. Physiologia Plantarum 70:196–202.
Chow, W. S., Goodchild, D. J., Miller, C., and Anderson, J. M. (1990a). The influence of high levels of brief or prolonged supplementary far-red illumination during growth on the photosynthetic characteristics, composition and morphology of Pisum sativum chloroplasts. Plant, Cell and Environment 13:135–145.
Chow, W. S., Melis, A., and Anderson, J. M. (1990b). Adjustments of photosystem stoichiometry in chloroplasts improve the quantum efficiency of photosynthesis. Proceedings of the National Academy of Sciences of the USA 87:7502–7506.
Coughlan, S. J. (1988). Chloroplast thylakoid protein phosphorylation is influenced by mutations in the cytochrome b-f complex. Biochimica et Biophysica Acta 933:413–422.
Cunningham, F. X., Dennenberg, R. J., Jursinic, P. A., and Gantt, E. (1990). Growth under red light enhances photosystem II relative to photosystem I and phycobilisomes in the red algae Porphyridium cruentum. Plant Physiology 93:888–895.
Darr, S. C., Somerville, S. C., and Arntzen, C. J. (1986). Monoclonal antibodies to the light harvesting chlorophyll a/b protein complex of photosystem II. Journal of Cell Biology 103:733–740.
Demeter, S., Neale, P. J., and Melis, A. (1987). Photoinhibition: impairment of the primary charge separation between P680 and pheophytin in photosystem II of chloroplasts. FEBS Letters 214:370–374.
Deng, X.-W., Tonkyn, J. C., Peter, G. F., Thornber, J. P., Gruissem, W. (1989). Post-transcriptional control of plastid mRNA accumulation during adaptation of chloroplasts to different light quality environments. Plant Cell 1:645–654.
Duysens, L. N. M., Amesz, J., and Kamp, B. M. (1961). Two photochemical systems in photosynthesis. Nature 190:510–511.
Elich, T. D., Edelman, M., and Mattoo, A. (1992). Identification, characterization, and resolution of the in vivo phosphorylated form of the D1 photosystem II reaction center protein. Journal of Biological Chemistry 267:3523–3529.
Emerson, R., and Arnold, W. (1932a). A separation of the reactions in photosynthesis by means of intermittent light. Journal of General Physiology 15:391–420.
Emerson, R., and Arnold, W. (1932b). The photochemical reactions in photosynthesis. Journal of General Physiology 16:191–205.
Escoubas, J. M., Lomas, M., LaRoche, J., and Falkowski, P. G. (1995). Light intensity regulation of cab gene transcription is signalled by the redox state of the plastoquinone pool. Proceedings of the National Academy of Sciences of the USA 92:10237–10241.
Evans, J. R. (1987). The dependence of quantum yield on wavelength and growth irradiance. Australian Journal of Plant Physiology 14:69–79.
Falbel, T., Meehl, J. B., and Staehelin, L. A. (1996). Severity of mutant phenotype in a series of chlorophyll-deficient wheat mutants depends on light intensity and the severity of the block in chlorophyll synthesis. Plant Physiology 112:821–832.
Fujita, Y., and Murakami, A. (1987). Regulation of electron transport composition in cyanobacterial photosynthetic system: stoichiometry among photosystem I and II complexes and their light-harvesting antennae and cytochrome b 6/f complex. Plant and Cell Physiology 28:1547–1553.
Fujita, Y., Ohki, K., and Murakami, A. (1985). Chromatic regulation of photosystem composition in the photosynthetic system of red and blue-green algae. Plant and Cell Physiology 26:1541–1548.
Fujita, Y., Iwama, Y., Ohki, K., Murakami, A., Hagiwara, N. (1989). Regulation of the size of light-harvesting antennae in response to light intensity in the green alga Chlorella pyrenoidosa. Plant and Cell Physiology 30:1029–1037.
Gaffron, H., and Wohl, K. (1936). Zur Theorie der Assimilation. Naturwissenschaften 24:81–90.
Glazer, A. N., and Melis, A. (1987). Photochemical reaction centers: structure, organization, and function. Annual Review of Plant Physiology 38:11–45.
Glick, R. E., and Melis, A. (1988). Minimum photosynthetic unit size in system-I and system-II of barley chloroplasts. Biochimica et Biophysica Acta 934:151–155.
Glick, R. E., McCauley, S. W., Gruissem, W., and Melis, A. (1986). Light quality regulates expression of chloroplast genes and assembly of photosynthetic membrane complexes. Proceedings of the National Academy of Sciences of the USA 83:4287–4291.
Guenther, J. E., Nemson, J. A., and Melis, A. (1990). Development of PSII in dark grown Chlamydomonas reinhardtii. A light-dependent conversion of PSIIβ, QB-nonreducing centers to the PSIJα, QB-reducing form. Photosynthesis Research 24:35–46.
Harrison, M. A., and Melis, A. (1992). Organization and stability of polypeptides associated with the chlorophyll a-b light-harvesting complex of photosystem II. Plant and Cell Physiology 33:627–637.
Haworth, P., Watson, J. L., and Arntzen, C. J. (1983). The detection, isolation and characterization of a light-harvesting complex which is specifically associated with photosystem I. Biochimica et Biophysica Acta 724:151–158.
Hill, R., and Bendall, F. (1960). Function of the two cytochrome components in chloroplasts: a working hypothesis. Nature 186:136–137.
Ikeuchi, M., Hirano, A., and Inoue, Y (1991). Correspondence of apoproteins of light-harvesting chlorophyll a/b complexes associated with photosystem-I to cab genes: evidence for a novel Type IV apoprotein. Plant and Cell Physiology 32:103–112.
Jansson, S., Pichersky, E., Bassi, R., Green, B. R., Ikeuchi, M., Melis, A., Simpson, D. J., Spangfort, M., Staehelin, L. A., Thornber, J. P. (1992). A nomenclature for the genes encoding the chlorophyll a/b-binding proteins of higher plants. Plant Molecular Biology Reports 10:242–253.
Kim, J. H., Glick, R. E., and Melis, A. (1993a). Dynamics of photosystem stoichiometry adjustment by light-quality in chloroplasts. Plant Physiology 102:181–190.
Kim, J. H., Nemson, J. A., and Melis, A. (1993b). Photosystem-II reaction center damage and repair in the green alga Dunaliella salina: analysis under physiological and adverse irradiance conditions. Plant Physiology 103:181–189.
Kirk, J. T. O. (1983). Light and Photosynthesis in Aquatic Ecosystems. Cambridge University Press, New York.
Knoetzel, J., Svendsen, I., and Simpson, D. J. (1992). Identification of the photosystem-I antenna polypeptides in barley Isolation of 3 pigment-binding antenna complexes. European Journal of Biochemistry 206:209–215.
Kühlbrandt, W., and Wang, D. N. (1991). Three-dimensional structure of plant light-harvesting complex determined by electron crystallography. Nature 350:130–134.
Kühlbrandt, W., Wang, D. N., and Fujiyoshi, Y. (1994). Atomic model of plant light-harvesting complex determined by electron crystallography. Nature 367:614–621.
Lam, E., Ortiz, W., Mayfield, S., and Malkin, R. (1984). Isolation and characterization of a light-harvesting chlorophyll a/b complex associated with photosystem I. Plant Physiology 74:650–655.
LaRoche, J., Mortain-Bertrand, A., and Falkowski, P. G. (1991). Light-intensity-induced changes in cab mRNA and light-harvesting complex II apoprotein levels in the unicellular chlorophyte Dunaliella tertiolecta. Plant Physiology 97:147–153.
Larsson, U. K., Anderson, J. M., and Andersson, B. (1987). Variations in the relative content of the peripheral and inner light-harvesting chlorophyll a/b-protein complex (LHC-II) subpopulations during thylakoid light adaptation and development. Biochimica et Biophysica Acta 894:69–75.
Leong, T. A., and Anderson, J. M. (1984). Adaptation of the thylakoid membranes of pea chloroplasts to light intensities. I. Study on the distribution of chlorophyll-protein complexes. Photosynthesis Research 5:105–115.
Ley, A. C., and Mauzerall, D. C. (1982). Absolute absorption cross sections for photosystem II and the minimum quantum requirement for photosynthesis in Chlorella vulgaris. Biochimica et Biophysica Acta 680:95–106.
Manodori, A., and Melis, A. (1986). Cyanobacterial acclimation to photosystem I or photosystem II light. Plant Physiology 82:185–189.
Mattoo, A. K., and Edelman, M. (1987). Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein. Proceedings of the National Academy of Sciences of the USA 84:1497–1501.
Mattoo, A., Hoffman-Falk, H., Marder, J., and Edelman, M. (1984). Regulation of protein metabolism: coupling of photosynthetic electron-transport to in vivo degradation of the rapidly metabolized 32-kDa protein of the chloroplast membranes. Proceedings of the National Academy of Sciences of the USA 81:1380–1384.
Mawson, B. T., Morrissey, P. J., Gomez, A., and Melis, A. (1994). Thylakoid membrane development and differentiation: assembly of the chlorophyll a-b light-harvesting complex and evidence for the origin of Mr = 19, 17.5 and 13.4 kDa proteins. Plant and Cell Physiology 35:341–151.
Melis, A. (1984). Light regulation of photosynthetic membrane structure, organization and function. Journal of Cellular Biochemistry 24:271–285.
Melis, A. (1991). Dynamics of photosynthetic membrane composition and function. Biochimica et Biophysica Acta 1058:87–106.
Melis, A. (1996). Excitation energy transfer: functional and dynamic aspects of Lhc (cab) proteins. In: Ort, D. R., and Yocum, C. F., eds. Oxygenic Photosynthesis: The Light Reactions. Kluwer Academic Publishers, Dordrecht, The Netherlands. pp. 523–538.
Melis, A., and Anderson, J. M. (1983). Structural and functional organization of the photosystems in spinach chloroplasts: antenna size, relative electron transport capacity, and chlorophyll composition. Biochimica et Biophysica Acta 724:473–484.
Melis, A., and Harvey, G. W. (1981). Regulation of photosystem stoichiometry, chlorophyll a and chlorophyll b content and relation to chloroplast ultrastructure. Biochimica et Biophysica Acta 637:138–145.
Melis, A., Mullineaux, C. W., and Allen, J. F. (1989). Acclimation of the photosynthetic apparatus to photosystem I or photosystem II light: evidence from quantum yield measurement and fluorescence spectroscopy of cyanobacterial cells. Zeitschrift für Naturforschung Teil C 44:109–118.
Melis, A., Murakami, A., Nemson, J. A., Aizawa, K., Ohki, K., and Fujita, Y. (1996). Chromatic regulation in Chlamydomonas reinhardtii alters photosystem stoichiometry and improves the quantum efficiency of photosynthesis. Photosynthesis Research 47:253–265.
Morrissey, P. J., Glick, R. E., and Melis, A. (1989). Supramolecular assembly and function of subunits associated with the chlorophyll a/b light-harvesting complex II (LHC-II) in soybean chloroplasts. Plant and Cell Physiology 30:335–344.
Murakami, A., and Fujita, Y. (1988). Steady state of photosynthesis in cyanobacterial photosynthetic systems before and after regulation of electron transport composition: overall rate of photosynthesis and PS I/PS II composition. Plant and Cell Physiology 29:305–311.
Murakami, A., and Fujita, Y. (1991). Steady state of photosynthetic electron transport in cells of the cyanophyte Synechocystis PCC 6714 having different stoichiometry between PSII and PSI: analysis of flash-induced oxidation-reduction of cytochrome f and P700 under steady state of photosynthesis. Plant and Cell Physiology 32:213–222.
Murakami, A., Nemson, J. A., Fujita, Y., and Melis, A. (1997). Chromatic regulation in Chlamydomonas reinhardtii: time course of photosystem stoichiometry adjustment following a shift in growth light quality. Plant and Cell Physiology 38:188–193.
Myers, J., Graham, J. R., and Wang, R. T. (1980). Light-harvesting in Anacystis nidulans studied in pigment mutants. Plant Physiology 66:1144–1149.
Nanba, O., and Satoh, K. (1987). Isolation of a photosystem-II reaction center consisting of D-1 and D-2 polypeptides and cytochrome 6-559. Proceedings of the National Academy of Sciences of the USA 84:109–112.
Neale, P. J., and Melis, A. (1990). Activation of a reserve pool of photosystem II in Chlamydomonas reinhardtii counteracts photoinhibition. Plant Physiology 92:1196–1204.
Ohtsuka, T., Ito, H., and Tanaka, A. (1997). Conversion of chlorophyll b to chlorophyll a and the assembly of chlorophyll with apoproteins by isolated chloroplasts. Plant Physiology 113:137–147.
Peter, G. F., and Thornber, J. P. (1991). Biochemical composition and organization of higher plant photosystem-II light-harvesting pigment-proteins. Journal of Biological Chemistry 266:16745–16754.
Pichersky, E., and Jansson, S. (1996). The light-harvesting chlorophyll a/b-binding polypeptides and their genes in angiosperm and gymnosperm species. In: Ort, D. R., and Yocum, C. F., eds. Oxygenic Photosynthesis: The Light Reactions. Kluwer Academic Publishers, Dordrecht, The Netherlands. pp. 507–521.
Powles, S. B. (1984). Photoinhibition of photosynthesis induced by visible light. Annual Review of Plant Physiology 35:15–44.
Salter, A. H., Virgin, I., Hagman, Å., Andersson, B. (1992). On the molecular mechanism of light-induced D1-protein degradation in photosystem-II core particles. Biochemistry 31:3990–3998.
Simpson, D. J., and Knoetzel, J. (1996). Light-harvesting complexes of plants and algae: introduction, survey and nomenclature. In: Ort, D. R., and Yocum, C. F., eds. Oxygenic Photosynthesis: The Light Reactions. Kluwer Academic Publishers, Dordrecht, The Netherlands. pp. 493–506.
Smith, B. M., Morrissey, P. J., Guenther, J. E., Nemson, J. A., Harrison, M. A., Allen, J. F., and Melis, A. (1990). Response of the photosynthetic apparatus in Dunaliella salina (green algae) to irradiance stress. Plant Physiology 93:1433–1440.
Sukenik, A., Bennett, J., and Falkowski, P. G. (1988). Changes in the abundance of individual apoproteins of light-harvesting chlorophyll a/b-protein complexes of photosystem I and II with growth irradiance in the marine chlorophyte Dunaliella tertiolecta. Biochimica et Biophysica Acta 932:206–215.
Terashima, I., and Saeki, T. (1983). Light environment within a leaf. I. Optical properties of paradermal sections of Camelia leaves with special reference to differences in the optical properties of palisade and spongy tissues. Plant and Cell Physiology 24:1493–1501.
Thornber, J. P., Peter, G. F., Chitnis, P. R., Nechushtai, R., and Vainstein, A. (1988). The light-harvesting complex of photosystem II of higher plants. In: Stevens, S. E. Jr., and Bryant, D. A., eds. Light-energy Transduction in Photosynthesis: Higher Plant and Bacterial Models. The American Society of Plant Physiologists, Rockville, Maryland. pp. 137–154.
Vogelmann, T. (1989). Penetration of light into plants. Photochemistry and Photobiology 50:895–902.
Vogelmann, T. C. (1993). Plant tissue optics. Annual Review of Plant Physiology and Plant Molecular Biology 44:231–251.
Webb, M. R., and Melis, A. (1995). Chloroplast response in Dunaliella salina to irradiance stress. Effect on thylakoid membrane assembly and function. Plant Physiology 107:885–893.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media New York
About this chapter
Cite this chapter
Melis, A. (1998). Photostasis in Plants. In: Williams, T.P., Thistle, A.B. (eds) Photostasis and Related Phenomena. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1549-8_13
Download citation
DOI: https://doi.org/10.1007/978-1-4899-1549-8_13
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-1551-1
Online ISBN: 978-1-4899-1549-8
eBook Packages: Springer Book Archive