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Pigment ligation to proteins of the photosynthetic apparatus in higher plants
Author(s) -
Paulsen Harald
Publication year - 1997
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1997.tb00003.x
Subject(s) - thylakoid , chlorophyll , photosynthesis , biochemistry , carotenoid , chlorophyll b , chloroplast , pigment , chlorophyll a , chemistry , light harvesting complex , biophysics , biology , membrane protein , membrane , botany , photosystem ii , organic chemistry , gene
Ligation of pigments to proteins of the thylakoid membrane is a central step in the assembly of the photosynthetic apparatus in higher plants. Because of the potentially damaging photooxidative activity of chlorophylls, it is likely that between their biosynthesis and final assembly, chlorophylls will always be bound to protein complexes in which photooxidation is prevented by quenchers such as carotenoids. Such complexes may include chlorophyll carriers and/or membrane receptors involved in protein insertion into the membrane. Many if not all pigment‐protein complexes of the thylakoid are stabilised towards protease attack by bound pigments. The major light‐harvesting chlorophyll a/b protein (Lhebl,2) folds into its native structure in vitro only when it binds pigments. Pigment‐induced folding may also be a general feature of chlorophyll‐carotenoid proteins of the photosynthetic apparatus.

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