ABSTRACT
We present an optically detected magnetic resonance (ODMR) and electron paramagnetic resonance (EPR) spectroscopic study on the quenching of photo-induced chlorophyll triplet states by carotenoids, in the intrinsic light-harvesting complex (LHC) from the dinoflagellate Amphidinium carterae. Two carotenoid triplet states, differing in terms of optical and magnetic spectroscopic properties, have been identified and assigned to peridinins located in different protein environment. The results reveal a parallelism with the triplet-triplet energy transfer (TTET) process involving chlorophyll a and luteins observed in the LHC-II complex of higher plants. Starting from the hypothesis of a conserved alignment of the amino acid sequences at the cores of the LHC and LHC-II proteins, the spin-polarized time-resolved EPR spectra of the carotenoid triplet states of LHC have been calculated by a method which exploits the conservation of the spin momentum during the TTET process. The analysis of the spectra shows that the data are compatible with a structural model of the core of LHC which assigns the photo-protective function to two central carotenoids surrounded by the majority of Chl a molecules present in the protein, as found in LHC-II. However, the lack of structural data, and the uncertainty in the pigment composition of LHC, leaves open the possibility that this complex posses a different arrangement of the pigments with specific centers of Chl triplet quenching.
Subject(s)
Electron Spin Resonance Spectroscopy/methods , Light-Harvesting Protein Complexes/chemistry , Magnetic Resonance Spectroscopy/methods , Protozoan Proteins/chemistry , Animals , Carotenoids/chemistry , Carotenoids/metabolism , Chlorophyll/chemistry , Chlorophyll/metabolism , Chlorophyll A , Dinoflagellida/chemistry , Dinoflagellida/metabolism , Energy Transfer/radiation effects , Light-Harvesting Protein Complexes/metabolism , Lutein/chemistry , Lutein/metabolism , Models, Molecular , Protein Conformation , Protozoan Proteins/metabolismABSTRACT
The Chlorophyll a (Chl a) molecules involved in the triplet-triplet energy transfer to the central luteins in trimeric LHC-II are identified by time-resolved and pulse EPR techniques. The concept of spin angular momentum conservation during triplet-triplet energy transfer is exploited for the calculation of the spin polarization of the carotenoid triplet states. The sites with the highest probability of forming triplet states, which are quenched by the central luteins, result to be Chl603 and Chl612. "Unquenched" Chl triplet states are produced by photoexcitation in the LHC-II complex. Putative sites of these triplet states are Chl614, Chl611, Chl604, and Chl613 since they do not contribute to the formation of the observed carotenoid triplet states.
