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

doi:10.1016/j.febslet.2006.08.049

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 journal › Article › peer-review

33 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 language	English
Pages (from-to)	5257-5262
Number of pages	6
Journal	FEBS Letters
Volume	580
Issue number	22
DOIs	https://doi.org/10.1016/j.febslet.2006.08.049
Publication status	Published - 2 Oct 2006

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title = "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.",

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T1 - Peridinin-chlorophyll-protein reconstituted with chlorophyll mixtures

T2 - Preparation, bulk and single molecule spectroscopy

AU - Brotosudarmo, T. H P

AU - Hofmann, E.

AU - Hiller, R. G.

AU - Wörmke, S.

AU - Mackowski, S.

AU - Zumbusch, A.

AU - Bräuchle, C.

AU - Scheer, H.

PY - 2006/10/2

Y1 - 2006/10/2

N2 - 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.

AB - 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.

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SN - 0014-5793

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SP - 5257

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JO - FEBS Letters

JF - FEBS Letters

IS - 22

ER -

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

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