Abstract
The zero-field fluorescence-detected triplet state magnetic resonance spectra have been obtained for the pyrochlorophyllide a—apomyoglobin complex at 2 K. The triplet state zero-field splittings and spin sublevel dynamics were detected on the resolved features of the structured low-temperature fluorescence. Structured fluorescence is not observed for pyrochlorophylide a in an organic matrix under identical conditions. These data are interpreted in terms of the local binding site of the pyrochlorophyllide a chromophore in the protein and the low-temperature conformation of the protein matrix.
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