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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Brotosudarmo TH,Hofmann E,Hiller RG,Wörmke S,Mackowski S,Zumbusch A,Bräuchle C,Scheer Hdoi
10.1016/j.febslet.2006.08.049subject
Has Abstractpub_date
2006-10-02 00:00:00pages
5257-62issue
22eissn
0014-5793issn
1873-3468pii
S0014-5793(06)01044-1journal_volume
580pub_type
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