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In photosynthesis, light is captured by antenna proteins. These proteins transfer the excitation energy with almost 100% quantum efficiency to the reaction centers, where charge separation takes place. The time scale and pathways of this transfer are controlled by the protein scaffold, which holds the pigments at optimal geometry and tunes their excitation(More)
The Fenna–Matthews–Olson (FMO) protein of green sulfur bacteria represents an important model protein for the study of elementary pigment–protein couplings. We have previously used a simple approach [Adolphs and Renger (2006) Biophys J 91:2778–2797] to study the shift in local transition energies (site energies) of the FMO protein of Prosthecochloris(More)
Using the 2.9 A resolution structure of the membrane-intrinsic protein-cofactor complex photosystem II (PSII) from the cyanobacterium Thermosynechococcus elongatus, we calculated and characterized nine possible substrate/product channels leading to/away from the Mn(4)Ca cluster, where water is oxidized to dioxygen, protons, and electrons. Five narrow(More)
The photosynthetic oxygen-evolving photosystem II (PSII) is the only known biochemical system that is able to oxidize water molecules and thereby generates almost all oxygen in the Earth's atmosphere. The elucidation of the structural and mechanistic aspects of PSII keeps scientists all over the world engaged since several decades. In this Minireview, we(More)
The effect of solubilization of photosynthetic reaction centers (RCs) from Rhodobacter sphaeroides with different detergents on the electronic structure of the oxidized primary donor, P.+, is investigated. Electron paramagnetic resonance spectroscopy and related multiple resonance techniques (ENDOR/Special TRIPLE) show that two distinct conformations of P.+(More)
The photosystem II core complex is the water:plastoquinone oxidoreductase of oxygenic photosynthesis situated in the thylakoid membrane of cyanobacteria, algae and plants. It catalyzes the light-induced transfer of electrons from water to plastoquinone accompanied by the net transport of protons from the cytoplasm (stroma) to the lumen, the production of(More)
The Fenna-Matthews-Olson (FMO) light-harvesting protein connects the outer antenna system (chlorosome/baseplate) with the reaction center complex in green sulfur bacteria. Since its first structure determination in the mid-70s, this pigment-protein complex has become an important model system to study excitation energy transfer. Recently, an additional(More)
The absorption properties of chlorophyll a (Chla) in active core complexes of photosystems I (PSI) and II (PSII) isolated in high purity from the thermophilic cyanobacterium Thermosynechococcus elongatus were correlated with those of extracts in 80% acetone to determine effective extinction coefficients of protein-bound Chla and molar extinction(More)
Optical line shape theory is combined with a quantum-chemical/electrostatic calculation of the site energies of the 96 chlorophyll a pigments and their excitonic couplings to simulate optical spectra of photosystem I core complexes from Thermosynechococcus elongatus. The absorbance, linear dichroism and circular dichroism spectra, calculated on the basis of(More)
The crystal structure of the class IIb water-soluble chlorophyll binding protein (WSCP) from Lepidium virginicum is used to model linear absorption and circular dichroism spectra as well as excited state decay times of class IIa WSCP from cauliflower reconstituted with chlorophyll (Chl) a and Chl b. The close agreement between theory and experiment suggests(More)