Relative binding affinities of chlorophylls in peridinin-chlorophyll- protein reconstituted with heterochlorophyllous mixtures

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

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    12 Citations (Scopus)

    Abstract

    Peridinin-chlorophyll-protein (PCP), containing differently absorbing chlorophyll derivatives, are good models with which to study energy transfer among monomeric chlorophylls (Chls) by both bulk and single-molecule spectroscopy. They can be obtained by reconstituting the N-terminal domain of the protein (N-PCP) with peridinin and chlorophyll mixtures. Upon dimerization of these "half-mers", homo- and heterochlorophyllous complexes are generated, that correspond structurally to monomeric protomers of native PCP from Amphidinium carterae. Heterochlorophyllous complexes contain two different Chls in the two halves of the complete structure. Here, we report reconstitution of N-PCP with binary mixtures of Chl a, Chl b, and [3-acetyl]-Chl a. The ratios of the pigments were varied in the reconstitution mixture, and relative binding constants were determined from quantification of these pigments in the reconstituted PCPs. We find higher affinities for both Chl b and [3-acetyl]-Chl a than for the native pigment, Chl a.

    Original languageEnglish
    Pages (from-to)247-252
    Number of pages6
    JournalPhotosynthesis Research
    Volume95
    Issue number2-3
    DOIs
    Publication statusPublished - Feb 2008

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