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Effect of the Protein Matrix of Cytochrome c in Suppressing the Inherent Peroxidase Activity of Its Heme Prosthetic Group
Author(s) -
Diederix Rutger E. M.,
Ubbink Marcellus,
Canters Gerard W.
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20020104)3:1<110::aid-cbic110>3.0.co;2-2
Subject(s) - heme , peroxidase , cytochrome c peroxidase , cofactor , chemistry , cytochrome , hemeprotein , biochemistry , enzyme , cytochrome c , electron transfer , stereochemistry , photochemistry , mitochondrion
Unraveling enzyme activity : Unfolding of the electron‐transfer protein cytochrome c ‐550 results in a spectacular increase in its peroxidase activity (see graph). This finding is interpreted in terms of the suppression by the cytochrome protein matrix of the potentially harmful peroxidase activity inherent to its heme cofactor.