| | Peridinin–chlorophyll–protein reconstituted with chlorophyll mixtures: Preparation, bulk and single molecule spectroscopyEdited by Miguel De la Rosa Received 23 July 2006; received in revised form 21 August 2006; accepted 24 August 2006. published online 04 September 2006. 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 32kDa 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. Abbreviations: A., Amphidinium, CD, circular dichroism, Chl, chlorophyll, EET, excitation energy transfer, l-PCP, large (32kDa PCP), N-PCP, N-terminal 16kDa-domain of PCP, PCP, peridinin–chlorophyll–protein, Per, peridinin, s-PCP, small (16kDa) PCP, SMS, single molecule spectroscopy a Department Biologie I – Bereich Botanik, Ludwig-Maximilians-Universität München, Menzinger Str. 67, D-80638 München, Germany b Department Chemie und Biochemie – Physikalische Chemie, and Center for Nanoscience, Ludwig-Maximilians Universität, München, Germany c Fakultät für Biologie, Biophysik, Ruhr Universität Bochum, Germany d Macquarie University, Sydney, Australia e Fachbereich Chemie, Universität Konstanz, Germany  Corresponding author. Fax: +49 89 17861 271.
PII: S0014-5793(06)01044-1 doi:10.1016/j.febslet.2006.08.049 © 2006 Federation of European Biochemical Societies | |
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ABSTRACT
