THE INFLUENCE OF THE PEPTIDE-CHAIN ON THE KINETICS AND STABILITY OF MICROPEROXIDASES

Citation
Jh. Spee et al., THE INFLUENCE OF THE PEPTIDE-CHAIN ON THE KINETICS AND STABILITY OF MICROPEROXIDASES, European journal of biochemistry, 241(1), 1996, pp. 215-220
Citations number
12
Categorie Soggetti
Biology
ISSN journal
00142956
Volume
241
Issue
1
Year of publication
1996
Pages
215 - 220
Database
ISI
SICI code
0014-2956(1996)241:1<215:TIOTPO>2.0.ZU;2-G
Abstract
Microperoxidases with increasing lengths of the peptide attached to th e heme moiety have been isolated after proteolytic digestion of horse- heart cytochrome c (microperoxidases 6, 8, and 11) and of cytochrome c (550) from Thiobacillus versutus (microperoxidase 17). The different m icroperoxidases catalyze the H2O2-dependent para-hydroxylation of anil ine relatively efficiently but are rapidly inactivated under turnover conditions. The horse-heart cytochrome-c-derived microperoxidases have identical values for V-max but show a decrease of the K-m for aniline and a higher stability when the attached peptide is longer. The kinet ic constants obtained for microperoxidase 17, differ markedly from the microperoxidases derived from horse-heart cytochrome c. Possible fact ors underlying the observed differences are discussed.