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Characterization of the Interactions of Fluorescent Probes with Proteins: Coumarin 153 and 1,8‐ANS in Complex with Holo‐ and Apomyoglobin
Author(s) -
Mukherjee Prasun,
Halder Mintu,
Hargrove Mark S.,
Petrich Jacob W.
Publication year - 2006
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.1751-1097.2006.tb09815.x
Subject(s) - coumarin , chemistry , fluorescence , solvation , crystallography , stereochemistry , solvent , biochemistry , organic chemistry , physics , quantum mechanics
In order to provide a thorough characterization of a system with which to study the dielectric response of a protein, a well‐defined system complex of a fluorescent probe and protein is required. We have argued that such a system is provided by coumarin 153 and apomyoglobin ( Photochem. Photobiol . 79, 440–446 [2004]). In order to demonstrate further that coumarin 153 exhibits negligible nonspecific binding to the surface of apomyoglobin, we study its interactions with both the apo and holo proteins. We further make a similar comparison with 8‐anilino‐l‐naphthalenesulfonic acid, for which an NMR structure with apomyoglobin has been obtained. Our results confirm the appropriateness of the system of coumarin 153 and apomyoglobin for the investigation of solvation by the protein matrix.