The Influence of the Peptide Chain on the Kinetics and Stability of Microperoxidases
Open Access
- 1 October 1996
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 241 (1) , 215-220
- https://doi.org/10.1111/j.1432-1033.1996.0215t.x
Abstract
Microperoxidases with increasing lengths of the peptide attached to the heme moiety have been isolated after proteolytic digestion of horse-heart cytochrome c (microperoxidases 6, 8, and 11) and of cytochrome c550 from Thiobacillus versutus (microperoxidase 17). The different microperoxidases catalyze the H2O2-dependent para -hydroxylation of aniline relatively efficiently but are rapidly inactivated under turnover conditions. The horse-heart cytochrome-c -derived microperoxidases have identical values for Vmax but show a decrease of the Km, for aniline and a higher stability when the attached peptide is longer. The kinetic constants obtained for microperoxidase 17, differ markedly from the microperoxidases derived from horse-heart cytochrome c. Possible factors underlying the observed differences are discussed.Keywords
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