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• W2014728075 abstract "Fluorescence-detected magnetic resonance of triplets in zero magnetic field (FDMR), fluorescence fading (FF) due to triplet-formation, both at 4.2 K, and prompt fluorescence decay kinetics (FDK) at room temperature have been measured for free pheophorbide-a (f-Pheo) and bound (b-Pheo) to a synthetic polypeptide (L-Lys-L-Ala-L-Ala)n, dissolved in dimethylformamide (DMF). Fluorescence decay kinetics measurements of f-Pheo in DMF yielded 1-5 ns lifetimes, for b-Pheo in DMF a ~ 50 ps decay-component was found emitting at 730–750 nm. Zero-field splitting parameters |D| and |E| of the lowest triplet state T1 were determined from FDMR spectra as (337 and 24) 10-4 cm-1 for f-Pheo and (359 and 25) 10-4 cm-1 for b-Pheo, both in DMF. Decay rate constants of the three spin levels of T1 of b-Pheo (Kx= 1200 50 s-1, ky= 440 25 s-1, kz= 80 5 s-1) and relative steady-state populations (Nx= 28 2%, Ny= 47 2%, Nz= 26 2%) determined from FF curves predict a fluorescence decrease at the D–E and D + E FDMR transitions, whereas experimentally a fluorescence increase is observed. The FDMR sign-inversion results from singlet-singlet energy transfer from b-Pheo monomers to their aggregates, followed by fast intersystem crossing to T1. These results indicate that aggregates are formed by two or more b-Pheo molecules at different positions on the folded polypeptide chain. This situation resembles that in chlorophyll-proteins, containing low-lying traps, resulting from interaction of chromophores with other chromophores and with the protein environment." @default.
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• W2014728075 date "1986-10-01" @default.
• W2014728075 modified "2023-10-18" @default.
• W2014728075 title "PICOSECOND LASER SPECTROSCOPY AND OPTICALLY DETECTED MAGNETIC RESONANCE ON A MODEL PHOTOSYNTHETIC SYSTEM" @default.
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• W2014728075 doi "https://doi.org/10.1111/j.1751-1097.1986.tb04703.x" @default.
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