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OXYGEN DIFFUSION THROUGH HORSERADISH PEROXIDASE
Author(s) -
Brunet Juan E.,
Jullian Carolina,
Jameson David M.
Publication year - 1990
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.1751-1097.1990.tb01742.x
Subject(s) - horseradish peroxidase , oxygen , peroxidase , chemistry , diffusion , biophysics , biochemistry , biology , organic chemistry , enzyme , physics , thermodynamics
— The quenching by molecular oxygen of the fluorescence from a protoporphyrin IX adduct of horseradish peroxidase has been investigated using both intensity and time‐resolved techniques. The bimolecular quenching rate constant determined for this process, as evaluated by the conventional Stern‐Volmer analysis, was 2 × 10 8 M −1 s −1 , among the lowest observed for protein systems. This result suggests that the heme binding site in horseradish peroxidase is relatively inaccessible to oxygen, which may account for the observation of room temperature phosphorescence in aerated solutions from enzymatically created triplet states.