Carotenoid to chlorophyll energy transfer in the peridinin-chlorophyll-a-protein complex involves an intramolecular charge transfer state
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چکیده
منابع مشابه
Carotenoid to chlorophyll energy transfer in the peridinin-chlorophyll-a-protein complex involves an intramolecular charge transfer state.
Carotenoids are, along with chlorophylls, crucial pigments involved in light-harvesting processes in photosynthetic organisms. Details of carotenoid to chlorophyll energy transfer mechanisms and their dependence on structural variability of carotenoids are as yet poorly understood. Here, we employ femtosecond transient absorption spectroscopy to reveal energy transfer pathways in the peridinin-...
متن کاملExcitation transfer in the peridinin-chlorophyll-protein of Amphidinium carterae.
Peridinin-chlorophyll-protein (PCP) is a unique light-harvesting protein that uses carotenoids as its primary light-absorbers. This paper theoretically investigates excitation transfer between carotenoids and chlorophylls in PCP of the dinoflagellate Amphidinium carterae. Calculations based on a description of the electronic states of the participating chromophores and on the atomic level struc...
متن کاملIdentification of excited-state energy transfer and relaxation pathways in the peridinin-chlorophyll complex: an ultrafast mid-infrared study.
The peridinin chlorophyll-a protein (PCP) is a water-soluble, trimeric light harvesting complex found in marine dinoflagellates that binds peridinin and Chl-a in an unusual stoichiometric ratio of 4:1. In this paper, the pathways of excited-state energy transfer and relaxation in PCP were identified by means of femtosecond visible-pump, mid-infrared probe spectroscopy. In addition, excited-stat...
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A series of linkers constructed from combinations of phenyl and ethynyl groups is shown to permit ultrafast energy transfer between two chlorophylls, while allowing control over radical cation migration between them.
متن کاملPeridinin chlorophyll a protein: relating structure and steady-state spectroscopy.
Peridinin chlorophyll a protein (PCP) from Amphidinium carterae has been studied using absorbance (OD), linear dichroism (LD), circular dichroism (CD), fluorescence emission, fluorescence anisotropy, fluorescence line narrowing (FLN), and triplet-minus-singlet spectroscopy (T-S) at different temperatures (4-293 K). Monomeric PCP binds eight peridinins and two Chls a. The trimeric structure of P...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2002
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.262537599