Kinetics of interconversion of redox intermediates of lactoperoxidase, eosinophil peroxidase and myeloperoxidase.
Myeloperoxidase, eosinophil peroxidase and lactoperoxidase are heme-containing oxidoreductases, which undergo a series of redox reactions. Though sharing functional and structural homology, reflecting their phylogenetic origin, differences are observed regarding their spectral features, substrate specificities, redox properties and kinetics of interconversion of the relevant redox intermediates ferric and ferrous peroxidase, compound I, compound II and compound III. Depending on substrate availability, these heme enzymes path through the halogenation cycle and/or the peroxidase cycle and/or act as poor (pseudo-) catalases.
Furtmüller
Paul Georg
PG
Metalloprotein Research Group, Division of Biochemistry, Department of Chemistry, BOKU-University of Natural Resources and Applied Life Sciences, Leipzig, Germany. christian.obinger@boku.ac.at
Jantschko
Walter
W
Zederbauer
Martina
M
Jakopitsch
Christa
C
Arnhold
Jurgen
J
Obinger
Christian
C
D000818:Animals; D047209:Eosinophil Peroxidase / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D007784:Lactoperoxidase / Q000737:chemistry / Q000378:metabolism*; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
D047209:Eosinophil Peroxidase; D007784:Lactoperoxidase; D009195:Peroxidase