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The molecular mechanism of the control of excitation energy dissipation in chloroplast membranes Inhibition of ΔpH‐dependent quenching of chlorophyll fluorescence by dicyclohexylcarbodiimide
Author(s) -
Ruban A.V.,
Walters R.G.,
Horton P.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81089-5
Subject(s) - thylakoid , quenching (fluorescence) , chemistry , chloroplast , protonation , photosystem ii , photochemistry , electron transport chain , membrane , chlorophyll fluorescence , biophysics , fluorescence , chlorophyll , electrochemical gradient , proton transport , photosynthesis , biochemistry , biology , organic chemistry , ion , physics , quantum mechanics , gene
Non‐radiative dissipation of absorbed excitation energy in chloroplast membranes is induced in the presence of the trans‐thylakoid proton motive force; this dissipation is measured as high energy state quenching of chlorophyll fluorescence. qE. It has been suggested that this results from a low pH‐induced structural alteration in the light harvesting complex of photosystem II, LHCII [(1991) FEBS Letters 292, 1–4], The effect of the carboxyl‐modifying agent, dicyclohexylcarbodiimide (DCCD). on energy dissipation in chloroplast membranes has been investigated. At concentrations below that required to Inhibit electron transport. DCCD caused a decrease in the steady state ΔpH, completely inhibited qE and also inhibited the low pH‐dependent induction of qE. DCCD binding to polypeptides in the 22–28 kDa range correlated with inhibition of qE. It is suggested that DCCD reacts with amino acids residues in LHCII whose protonation is the primary event in the induction of energy dissipation. This LHCII domain may be identical to one forming a proton channel linking the site of PSII‐dependent water oxidation to the thylakoid lumen [(1990) Eur. J. Biochem. 193, 731–736].