CoChat
Sign Up
Cited by 364Metal-Catalyzed Oxygenation MechanismsHemoglobin structure and functionNeutrophil, Myeloperoxidase and Oxidative Mechanisms

Active site structure and catalytic mechanisms of human peroxidases

Furtmüller, Paul G., Zederbauer, Martina, Jantschko, Walter, Helm, Jutta, Bogner, Martin, Jakopitsch, Christa, Obinger, Christian·2006·Archives of Biochemistry and Biophysics
DOI 10.1016/j.abb.2005.09.017
Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1016/j.abb.2005.09.017

Cites

123 of 123 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • SCN− is not considered a biologically functional ion, but it plays an important role as a substrate for peroxidase enzymes, which form an essential part of innate defense, including LPO, SPO, MPO and EPO.

    “In general, SCN− is not considered a biologically functional ion, but it plays an important role as a substrate for peroxidase enzymes, which form an essential part of innate defense, including lactoperoxidase LPO, salivary peroxidase SPO, myeloperoxidase MPO and eosinophilic peroxidase EPO [172].”

    From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [172]

  • These peroxidases catalyze the oxidation of halides and pseudohalides by H2O2, resulting in potent oxidizing agents that exhibit antimicrobial activity in vitro and in vivo by damaging vital structural and functional components of microorganisms.

    “These peroxidases catalyze the oxidation of halides (Cl−, Br−, I−) and pseudohalides (SCN−) by H2O2, resulting in potent oxidizing agents that exhibit antimicrobial activity in vitro and in vivo, as they damage vital structural and functional components of microorganisms.”

    From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [172]

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Related

Authors
Furtmüller, P. G., Zederbauer, M., Jantschko, W., Helm, J., Bogner, M., Jakopitsch, C., & Obinger, C.
Corresponding author
Obinger, Christian
ORCID
Venue
Archives of Biochemistry and Biophysics
Publisher
Elsevier BV
Published
2006-01
Volume
445
Issue
2
Pages
199-213
ISSN
0003-9861 (ISSN-L)
DOI
10.1016/j.abb.2005.09.017
OpenAlex
W2021171040
Cited by
358
References
123
Citations by year
2026: 8 · 2025: 11 · 2024: 16 · 2023: 10 · 2022: 18 · 2021: 16 · 2020: 22 · 2019: 18 · 2018: 14 · 2017: 18 · 2016: 13 · 2015: 21 · 2014: 27 · 2013: 21 · 2012: 23
FWCI
1.34
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Archives of Biochemistry and Biophysics (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Keywords
myeloperoxidase, eosinophil peroxidase, lactoperoxidase, thyroid peroxidase, heme peroxidase, active site structure, catalytic mechanism, compound I, compound II, compound III, structure-function relationship, substrate specificity, host defense, hormone biosynthesis
MeSH terms
Amino Acid Sequence, Binding Sites, Catalysis, Enzyme Activation, Humans, Molecular Sequence Data, Peroxidases, Protein Conformation, Structure-Activity Relationship, Substrate Specificity

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review