Energy transfer in a light-harvesting carotenoid-chlorophyll c-chlorophyll a-protein of Phaeodactylum tricornutum
1981
Gugliemelli, L.A. | Dutton, H.J. | Jursinic, P.A. | Siegelman, H.W.
The marine diatom P. tricornutum was readily disrupted in 0.1 N Tris-HCl buffer, pH 7.8, in a Braun Model MSK cell homogenizer at 0-5.degree. C. Treatment of the suspension with sodium lauryol sarcosinate (3 molecules/10,000 daltons of protein) at 5.degree. C in the dark and subsequent centrifugations produced a pigmented, protein fraction whose excitation spectrum exhibited energy transfer from carotenoids to chlorophyll a (Chl a). Disruption of the pigment-protein complex by heating in sodium dodecyl sulfate resulted in loss of energy transfer. For each Chl a molecule this fraction had 1 Chl 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. Based on Chl a concentrations, this fraction had .apprx. 18 times more apparent emission at 680 nm when excited at 470 nm than the intact cells.
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