Journal
FEBS LETTERS
Volume 581, Issue 13, Pages 2429-2433Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2007.04.056
Keywords
cyanobacteria; fluorescence; non-photochemical; quenching; phycobilisome; protein folding
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An inquiry into the effect of temperature on carotenoid triggered quenching of phycobilisome (PBS) fluorescence in a photosystem II-deficient mutant of Synechoeystis sp. results in identification of two temperature-dependent processes: one is responsible for the quenching rate, and one determines the yield of PBS fluorescence. Non-Arrhenius behavior of the light-on quenching rate suggests that carotenoid-absorbed light triggers a process that bears a strong resemblance to soluble protein folding, showing temperature-dependent enthalpy of activated complex formation. The response of PBS fluorescence yield to hydration changing additives and to passing of the membrane lipid phase transition point indicates that the pool size of PBSs subject to quenching depends on the state of some membrane component. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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