Authors: S Mackowski S Wörmke T H P Brotosudarmo H Scheer C Bräuchle
Publish Date: 2007/10/31
Volume: 95, Issue: 2-3, Pages: 253-260
Abstract
Peridinin–chlorophyll–proteins PCP were reconstituted with binary 11 chlorophyll Chl mixtures of Chl a Chl b 3–acetylChl a acChl a and studied by bulk and singlemolecule fluorescence spectroscopy The latter provides a way to distinguish in a given sample heterochlorophyllous complexes that contain two different Chls from homochlorophyllous ones containing the same Chl in both binding sites The results are compared with those of homochlorophyllous PCP reconstituted with pure Chl a Chl b or acChl a Relative intensities of the Chl fluorescence in heterochlorophyllous complexes were obtained and modeled using the Förster description of energy transfer combined with known variations of peridinin Per–Chl excitation transfer rates for the different Chl pigments In the case of heterochlorophyllous complexes containing acChl a the energy transfer is unidirectional in the energetically preferable direction while it is bidirectional in the sample reconstituted with Chl a and Chl bThe authors thank Roger Hiller for providing purified peridinin used in the reconstitution The work was supported by the Deutsche Forschungsgemeinschaft Bonn SFB 533 projects A6 and B7 S M acknowledges financial support from the Alexander von Humboldt Foundation
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