Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols.
Journal
Chemical reviews
ISSN: 1520-6890
Titre abrégé: Chem Rev
Pays: United States
ID NLM: 2985134R
Informations de publication
Date de publication:
09 10 2019
09 10 2019
Historique:
pubmed:
10
9
2019
medline:
25
7
2020
entrez:
10
9
2019
Statut:
ppublish
Résumé
Life on Earth evolved in the presence of hydrogen peroxide, and other peroxides also emerged before and with the rise of aerobic metabolism. They were considered only as toxic byproducts for many years. Nowadays, peroxides are also regarded as metabolic products that play essential physiological cellular roles. Organisms have developed efficient mechanisms to metabolize peroxides, mostly based on two kinds of redox chemistry, catalases/peroxidases that depend on the heme prosthetic group to afford peroxide reduction and thiol-based peroxidases that support their redox activities on specialized fast reacting cysteine/selenocysteine (Cys/Sec) residues. Among the last group, glutathione peroxidases (GPxs) and peroxiredoxins (Prxs) are the most widespread and abundant families, and they are the
Identifiants
pubmed: 31498605
doi: 10.1021/acs.chemrev.9b00371
doi:
Substances chimiques
Peroxides
0
Sulfhydryl Compounds
0
Hydrogen Peroxide
BBX060AN9V
Peroxiredoxins
EC 1.11.1.15
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM