Journal of Plant Physiology 168 (2011) 1462–1472 Contents lists available at ScienceDirect Journal of Plant Physiology j ourna l ho mepage: www.elsevier.de/jplph Review Water soluble chlorophyll binding protein of higher plants: A most suitable model system for basic analyses of pigment–pigment and pigment–protein interactions in chlorophyll protein complexes G. Renger a,∗ , J. Pieper a,1 , C. Theiss b , I. Trostmann c , H. Paulsen c , T. Renger d , H.J. Eichler b , F.-J. Schmitt b a Max Volmer Laboratory for Biophysical Chemistry, Berlin Institute of Technology, 10523 Berlin, Germany b Institute of Optics and Atomic Physics, Berlin Institute of Technology, Germany c Institute of General Botany, Johannes Gutenberg University Mainz, Germany d Institute of Theoretical Physics, Johannes Kepler University Linz, Austria a r t i c l e i n f o Article history: Received 12 October 2010 Received in revised form 8 December 2010 Accepted 8 December 2010 Keywords: Pigment–pigment interaction Pigment–protein interaction Water soluble chlorophyll binding protein Fluorescence spectroscopy Hole burning spectroscopy Excitonic coupling Intersystem crossing a b s t r a c t This short review paper describes spectroscopic studies on pigment–pigment and pigment–protein inter- actions of chlorophyll (Chl) a and b bound to the recombinant protein of class IIa water soluble chlorophyll protein (WSCP) from cauliflower. Two Chls form a strongly excitonically coupled open sandwich dimer within the tetrameric protein matrix. In marked contrast to the mode of excitonic coupling of Chl and bacterio-Chl molecules in light harvesting complexes and reaction centers of all photosynthetic organ- isms, the unique structural pigment array in the Chl dimer of WSCP gives rise to an upper excitonic state with a large oscillator strength. This property opens the way for thorough investigations on exciton relaxation processes in Chl–protein complexes. Lifetime measurements of excited singlet states show that the unusual stability towards photodamage of Chls bound to WSCP, which lack any protective carotenoid molecule, originates from a high diffusion barrier to interaction of molecular dioxygen with Chl triplets. Site selective spectroscopic methods provide a wealth of information on the interactions of the Chls with the protein matrix and on the vibronic structure of the pigments. The presented data and discussions illustrate the great potential of WSCP as a model system for sys- tematic experimental and theoretical studies on the functionalizing of Chls by the protein matrix. It opens the way for further detailed analyses and a deeper understanding of the properties of pigment protein complexes. © 2011 Elsevier GmbH. All rights reserved. Contents Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1463 Water soluble chlorophyll proteins in plants . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1463 Spectral properties and theoretical modelling of the pigment–pigment interaction in class IIa WSCP . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1463 Excited state dynamics of class IIa WSCP . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1464 Lifetimes of excited singlet states in homo- and hetero-dimers of class IIa WSCP . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1466 Temperature dependence of excited singlet state lifetimes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1467 Effect of temperature on intersystem crossing of Chl a and Chl b . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1469 “Radiative” lifetime and transition dipole moment orientation in Chl . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1469 Pigment–protein interaction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1470 Concluding remarks and future perspectives . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1471 Acknowledgements . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1471 References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1471 ∗ Corresponding author. Tel.: +49 30 31422794; fax: +49 30 31421122. E-mail address: gernot.renger@mailbox.tu-berlin.de (G. Renger). 1 Present address: Institute of Physics, University of Tartu, Estonia. 0176-1617/$ – see front matter © 2011 Elsevier GmbH. All rights reserved. doi:10.1016/j.jplph.2010.12.005