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

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 Lett

journal_title

FEBS letters

authors

Brotosudarmo TH,Hofmann E,Hiller RG,Wörmke S,Mackowski S,Zumbusch A,Bräuchle C,Scheer H

doi

10.1016/j.febslet.2006.08.049

subject

Has Abstract

pub_date

2006-10-02 00:00:00

pages

5257-62

issue

22

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)01044-1

journal_volume

580

pub_type

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