Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes.

Redox Biol

LAQV, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal.

Published: October 2018

AI Article Synopsis

  • - Nitric oxide (NO) is a crucial signaling molecule involved in various body processes, with a new nitrate-nitrite-NO pathway identified as an alternative to the traditional NO formation from L-arginine, especially under low oxygen conditions.
  • - Under hypoxic conditions, nitrite can be converted back to NO, which protects cells during challenging situations, utilizing specific metalloproteins in mammalian cells known as "non-dedicated nitrite reductases."
  • - This review focuses on two non-dedicated nitrite reductases, xanthine oxidoreductase and aldehyde oxidase, examining their roles in NO metabolism based on in vitro and in vivo research findings.

Article Abstract

Nitric oxide radical (NO) is a signaling molecule involved in several physiological and pathological processes and a new nitrate-nitrite-NO pathway has emerged as a physiological alternative to the "classic" pathway of NO formation from L-arginine. Since the late 1990s, it has become clear that nitrite can be reduced back to NO under hypoxic/anoxic conditions and exert a significant cytoprotective action in vivo under challenging conditions. To reduce nitrite to NO, mammalian cells can use different metalloproteins that are present in cells to perform other functions, including several heme proteins and molybdoenzymes, comprising what we denominated as the "non-dedicated nitrite reductases". Herein, we will review the current knowledge on two of those "non-dedicated nitrite reductases", the molybdoenzymes xanthine oxidoreductase and aldehyde oxidase, discussing the in vitro and in vivo studies to provide the current picture of the role of these enzymes on the NO metabolism in humans.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6129670PMC
http://dx.doi.org/10.1016/j.redox.2018.08.020DOI Listing

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