Peridinin-chlorophyll-protein reconstituted with chlorophyll mixtures: Preparation, bulk and single molecule spectroscopy

T. H P Brotosudarmo, E. Hofmann, R. G. Hiller, S. Wörmke, S. Mackowski, A. Zumbusch, C. Bräuchle, H. Scheer*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    30 Citations (Scopus)

    Abstract

    Reconstitution of the 16 kDa N-terminal domain of the peridinin-chlorophyll-protein, N-PCP, with mixtures of chlorophyll a (Chl a) and Chl b, resulted in 32 kDa complexes containing two pigment clusters, each bound to one N-PCP. Besides homo-chlorophyllous complexes, hetero-chlorophyllous ones were obtained that contain Chl a in one pigment cluster, and Chl b in the other. Binding of Chl b is stronger than that of the native pigment, Chl a. Energy transfer from Chl b to Chl a is efficient, but there are only weak interactions between the two pigments. Individual homo- and hetero-chlorophyllous complexes were investigated by single molecule spectroscopy using excitation into the peridinin absorption band and scanning of the Chl fluorescence, the latter show frequently well resolved emissions of the two pigments.

    Original languageEnglish
    Pages (from-to)5257-5262
    Number of pages6
    JournalFEBS Letters
    Volume580
    Issue number22
    DOIs
    Publication statusPublished - 2 Oct 2006

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