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THE DISTANCE BETWEEN THE PHYTOCHROME CHROMOPHORE AND THE N‐TERMINAL CHAIN DECREASES DURING PHOTOTRANSFORMATION. A NOVEL FLUORESCENCE ENERGY TRANSFER METHOD USING LABELED ANTIBODY FRAGMENTS
Author(s) -
Farrens David L.,
Cordonnier MarieMichèle,
Pratt Lee H.,
Song PillSoon
Publication year - 1992
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1992.tb02227.x
Subject(s) - chromophore , fluorescence , phytochrome , chemistry , förster resonance energy transfer , photochemistry , kilodalton , energy transfer , biophysics , green fluorescent protein , fluorescent protein , biochemistry , optics , chemical physics , biology , physics , red light , botany , gene
— A novel antibody‐fluorescence method has been developed to elucidate the chromophore topography in phytochrome as it undergoes a photochromic transformation. Förster energy transfer from N‐terminal bound, fluorescently labeled Oat‐25 Fab antibody fragments to the phytochrome chromophore was measured. The results suggest that the chromophore moves relative to the N‐terminus upon the Pr → Pfr phototransformation. This conclusion is consistent with previous models which have proposed a reorientation and an interaction of the Pfr chromophore with the N‐terminus. The method described appears to be the first study of a Forster energy transfer measurement using a donor‐label attached to a Fab fragment of a photosensor protein.