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
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

Pagination

10829-10855

Auteurs

Darío A Estrin (DA)

Departamento de Química Inorgánica, Analítica y Química-Física and INQUIMAE-CONICET , Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires , 2160 Buenos Aires , Argentina.

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Classifications MeSH