Pigment−Pigment and Pigment−Protein Interactions in Recombinant Water-Soluble Chlorophyll Proteins (WSCP) from Cauliflower
Plants contain water-soluble chlorophyll-binding proteins (WSCPs) that function neither as antennas nor as components of light-induced electron transfer of photosynthesis but are likely constituents of regulatory protective pathways in particular under stress conditions. This study presents results on the spectroscopic properties of recombinant WSCP from cauliflower reconstituted with chlorophyll b (Chl b) alone or with mixtures of Chl a and Chl b. Two types of experiments were performed:? (a) measurements of stationary absorption spectra at 77 and 298 K and CD spectra at 298 K and (b) monitoring of laser flash-induced transient absorption changes with a resolution of 200 fs in the time domain of up to 100 ps. On the basis of a theoretical analysis outlined by Renger et al. (J. Phys. Chem. B 2007, 111, 10487) the data obtained in part (a) are interpreted within a model where tetrameric WSCP binds predominantly two Chl molecules in the form of an excitonically coupled ?open sandwich? dimer with a tilt angle of about 30° between the chlorin planes. The time-resolved measurements on Chl a/Chl b heterodimers are described by two exponential kinetics with time constants of 400 fs and 7 ps. These kinetics are assumed to reflect a heterogeneous population of WSCPs with Chl dimers either in excitonic coupled ?open sandwich? or weakly coupled geometric arrays. The 400 fs component is assigned to excited-state relaxations from the upper to the lower excitonic level of the strongly coupled ?open sandwich? dimer, while the 7?8 ps component probably indicates excitation energy transfer from 1Chl b* to Chl a in a dimer array with weak coupling due to significantly longer mutual distances between the chlorin rings.