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ENERGY TRANSFER IN A LIGHT‐HARVESTING CAROTENOID‐CHLOROPHYLL c ‐CHLOROPHYLL a ‐PROTEIN OF PHAEODACTYLUM TRICORNUTUM
Author(s) -
Gugliemelli L. A.,
Dutton H. J.,
Jursinic P. A.,
Segelman H. W.
Publication year - 1981
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1981.tb05510.x
Subject(s) - phaeodactylum tricornutum , fucoxanthin , xanthophyll , chlorophyll , chemistry , fluorescence , photosynthetic reaction centre , photosystem ii , chlorophyll a , biochemistry , pigment , chlorophyll c , photochemistry , biophysics , carotenoid , photosynthesis , biology , chromatography , botany , chlorophyll fluorescence , diatom , organic chemistry , physics , quantum mechanics
— The marine diatom Phaeodactylum tricornutum was readily disrupted in 0.1 N Tris‐HCl buffer, pH 7.8, in a Braun Model MSK cell homogenizer at 0‐5°C. Treatment of the suspension with sodium lauryol sarcosinate (3 molecules per 10000 daltons of protein) at 5°C in the dark and subsequent centrifugations produced a pigmented, protein fraction whose excitation spectrum exhibited energy transfer from carotenoids to chlorophyll a (Chi a ). Disruption of the pigment‐protein complex by heating in 1% sodium dodecylsulfate resulted in loss of energy transfer. For each Chi a molecule this fraction had 1 Chi c , 4 fucoxanthin, and 6.7 accessory pigment molecules. Presence of the accessory complex of Photosystem II in this preparation is suggested by the high xanthophyll content. Further, based on Chl a concentrations, this fraction had about 18 times more apparent fluorescence emission at 680 nm when excited at 470 nm than the intact cells.