Active site structure and catalytic mechanisms of human peroxidases.

Abstract:

:Myeloperoxidase (MPO), eosinophil peroxidase, lactoperoxidase, and thyroid peroxidase are heme-containing oxidoreductases (EC 1.7.1.11), which bind ligands and/or 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. Based on the published crystal structures of free MPO and its complexes with cyanide, bromide and thiocyanate as well as on sequence analysis and modeling, we critically discuss structure-function relationships. This analysis highlights similarities and distinguishing features within the mammalian peroxidases and intents to provide the molecular and enzymatic basis to understand the prominent role of these heme enzymes in host defense against infection, hormone biosynthesis, and pathogenesis.

journal_name

Arch Biochem Biophys

authors

Furtmüller PG,Zederbauer M,Jantschko W,Helm J,Bogner M,Jakopitsch C,Obinger C

doi

10.1016/j.abb.2005.09.017

subject

Has Abstract

pub_date

2006-01-15 00:00:00

pages

199-213

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(05)00403-0

journal_volume

445

pub_type

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