How does protein phosphorylation regulate photosynthesis?.
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How does protein phosphorylation regulate photosynthesis?. by John F. Allen

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Published by Elsevier in Amsterdam .
Written in English


Book details:

Edition Notes

Photocopy of: Trends in biochemical sciences, vol. 17, (1992), pp.12-17.

Other titlesTrends in biochemical sciences.
ContributionsInternational Union of Biochemistry.
ID Numbers
Open LibraryOL16546490M

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How does protein phosphorylation regulate photosynthesis? Allen JF(1). Author information: (1)Department of Biology, University of Oslo, Norway. Comment in Trends Biochem Sci. Sep;17(9) Phosphorylation of light-harvesting antenna proteins redirects absorbed light energy between reaction centres of photosynthetic by: How does protein phosphorylation regulate photosynthesis? IN PLANTS and photosynthetic bac- teria, phosphorylation of membrane proteins is ultimately responsible for many of the physiological responses to changes in incident light and redox poise 1,2. A major protein substrate of. Phosphorylation of light-harvesting antenna proteins redirects absorbed light energy between reaction centres of photosynthetic membranes. A generally accepted explanation for this is that electrostatic forces drive the more negatively charged, phosphorylated antenna proteins between membrane domains that differ in surface charge. However, structural studies on soluble phosphoproteins indicate Cited by: Fig. 1. A naive view of protein kinase and phosphatase reactions catalyzing phosphorylation and dephosphorylation of a threonyl residue. phosphorylation on molecular shape and bond geome­.

Abstract. The light-harvesting chlorophyll a / b complex (LHC II) of green plant chloroplasts accounts for about half the chlorophyll and a third of the protein of the thylakoid membrane (1,2). For each polypeptide of between 24 and 27 kDa, the complex contains 4 chlorophyll a molecules, 3 chlorophyll b molecules and 1–2 xanthophyll molecules. Each polypeptide is encoded by one of a family.   Phosphorylation is the chemical addition of a phosphoryl group (PO 3-) to an organic removal of a phosphoryl group is called dephosphorylation. Both phosphorylation and dephosphorylation are carried out by enzymes (e.g., kinases, phosphotransferases). Phosphorylation is important in the fields of biochemistry and molecular biology because it's a key reaction in protein and . Solar power. Figure \(\PageIndex{3}\): Overview of photosynthesis. Wikipedia. The answer is the captured energy of the photons from the sun (Figure ), which elevates electrons to an energy where they move “downhill” to their NADPH destination in a Z-shaped scheme. from book Regulation of Photosynthesis Thylakoid protein phosphorylation regulates state transition and PSII protein turnover under light-dependent redox control via a signal transduction.

Towards a comprehensive understanding of dynamic photosynthesis. Plant physiology and metabolism are fueled by sunlight. The essential biological process, which harnesses light to produce metabolic energy and oxygen, is coined photosynthesis. Phosphorylation regulates protein function and cell signaling by causing conformational changes in the phosphorylated protein. These changes can affect the protein in two ways. First, conformational changes regulate the catalytic activity of the protein. Thus, a protein can be either activated or inactivated by phosphorylation. (August ) As early as the 19th century it was known that phosphates could be bound to proteins. Most examples of these 'phosphoproteins' were found in milk (caseins) and egg yolk (phosvitin) and were simply considered a biological method of providing phosphorus as a nutrient. Therefore, the existence of phosphoproteins was considered a consequence of metabolic reactions, and nothing more. Thylakoid membranes in land plant chloroplasts are organized into appressed and nonappressed membranes, which contribute to the control of energy distribution between the two photosystems (PSI and PSII) from the associated light-harvesting complexes (LHCs). Under fluctuating light conditions, fast reversible phosphorylation of the N-terminal thylakoid protein domains and changes in.