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Protoporphyrin IX potentiates horseradish peroxidase‐catalyzed oxidation of NADH:Involvement of enzyme‐porphyrin interaction
Author(s) -
Sil Susmita,
Chakraborti Abhay S.
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203191
Subject(s) - horseradish peroxidase , chemistry , porphyrin , peroxidase , protoporphyrin ix , hydrogen peroxide , photochemistry , catalysis , protoporphyrin , enzyme , biochemistry , organic chemistry , photodynamic therapy
Protoporphyrin IX potentiates horseradish peroxidase‐catalyzed hydrogen peroxide‐mediated NADH oxidation, but the porphyrin cannot change the enzyme‐catalyzed o‐dianisidine oxidation. Spectrofluorimetric studies reveal that an interaction occurs between horseradish peroxidase and protoporphyrin IX. The interaction is predominantly hydrophobic and entropy‐driven endothermic process. This interaction may influence the potentiation effect of the protoporphyrin IX on horseradish peroxidase‐catalyzed NADH oxidation because the latter has a positive correlation with the extent of binding of the protein with the porphyrin.