ENERGY TRANSFER IN A LIGHT‐HARVESTING CAROTENOID‐CHLOROPHYLL c‐CHLOROPHYLL a‐PROTEIN OF PHAEODACTYLUM TRICORNUTUM

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Abstract
Abstract— 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.

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