Spectroscopic properties of the CP43 core antenna protein of photosystem II

ML Groot, RN Frese, FL de Weerd, K. Bromek, A. Pettersson, EJG Peterman, IHM van Stokkum, R van Grondelle, JP Dekker

Research output: Contribution to JournalArticleAcademicpeer-review


CP43 is a chlorophyll-protein complex that funnels excitation energy from the main light-harvesting system of photosystem II to the photochemical reaction center. We purified CP43 from spinach photosystem II membranes in the presence of the nonionic detergent n-dodecyl-β,d-maltoside and recorded its spectroscopic properties at various temperatures between 4 and 293 K by a number of polarized absorption and fluorescence techniques, fluorescence line narrowing, and Stark spectroscopy. The results indicate two “red” states in the Qy absorption region of the chlorophylls. The first peaks at 682.5 nm at 4 K, has an extremely narrow bandwidth with a full width at half-maximum of ∼2.7 nm (58 cm−1) at 4 K, and has the oscillator strength of a single chlorophyll. The second peaks at ∼679 nm, has a much broader bandshape, is caused by several excitonically interacting chlorophylls, and is responsible for all 4 K absorption at wavelengths longer than 685 nm. The Stark spectrum of CP43 resembles the first derivative of the absorption spectrum and has an exceptionally small overall size, which we attribute to opposing orientations of the monomer dipole moments of the excitonically coupled pigments.
Original languageEnglish
Pages (from-to)3328-3340
JournalBiophysical Journal
Issue number6
Publication statusPublished - Dec 1999


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