Natural mutations of human XDH promote the nitrite (NO2−)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health?-Reference-Cited by-同舟云学术

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Natural mutations of human XDH promote the nitrite (NO2−)-reductase capacity of xanthine oxidoreductase: A novel mechanism to promote redox health?

Published:2023-11 Issue: Volume:67 Page:102864
ISSN:2213-2317
Container-title:Redox Biology
language:en
Short-container-title:Redox Biology

Author:

Massimo G.,Khambata R.S.,Chapman T.,Birchall K.,Raimondi C.,Shabbir A.,Dyson Nicki,Rathod K.S.,Borghi C.,Ahluwalia A.^ORCID

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,Clinical Biochemistry

Reference66 articles.

1. The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme;Corte;Biochem. J.,1972

2. Mechanism of the conversion of xanthine dehydrogenase to xanthine oxidase: identification of the two cysteine disulfide bonds and crystal structure of a non-convertible rat liver xanthine dehydrogenase mutant;Nishino;J. Biol. Chem.,2005

3. Studies on xanthine oxidase: the dynamics of the oxidase system;Dixon;Biochem. J.,1924

4. Flavoprotein structure and mechanism. 4. Xanthine oxidase and xanthine dehydrogenase;Hille;Faseb. J.,1995

5. NADH oxidase activity of human xanthine oxidoreductase--generation of superoxide anion;Sanders;Eur. J. Biochem.,1997

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