Reciprocal regulation of sulfite oxidation and nitrite reduction by mitochondrial sulfite oxidase.
Molybdenum cofactor
Nitrate-nitrite-NO pathway
Nitric oxide
Nitrite reduction
Sulfite oxidase
Journal
Nitric oxide : biology and chemistry
ISSN: 1089-8611
Titre abrégé: Nitric Oxide
Pays: United States
ID NLM: 9709307
Informations de publication
Date de publication:
01 08 2019
01 08 2019
Historique:
received:
20
03
2019
revised:
08
04
2019
accepted:
11
04
2019
pubmed:
20
4
2019
medline:
7
5
2020
entrez:
20
4
2019
Statut:
ppublish
Résumé
The oxygen-independent nitrate-nitrite-nitric oxide (NO) pathway is considered as a substantial source of NO in mammals. Dietary nitrate/nitrite are distributed throughout the body and reduced to NO by the action of various enzymes. The intermembrane spaced (IMS), molybdenum cofactor-dependent sulfite oxidase (SO) was shown to catalyze such a nitrite reduction. In this study we asked whether the primary function of SO - sulfite oxidation - and its novel function - nitrite reduction - impact each other. First, we utilized benzyl viologen as artificial electron donor to investigate steady state NO synthesis by SO and found fast (k
Identifiants
pubmed: 31002874
pii: S1089-8603(19)30098-9
doi: 10.1016/j.niox.2019.04.004
pii:
doi:
Substances chimiques
Mitochondrial Proteins
0
Nitrites
0
Sulfites
0
Benzyl Viologen
13096-46-3
Heme
42VZT0U6YR
Oxidoreductases Acting on Sulfur Group Donors
EC 1.8.-
SUOX protein, human
EC 1.8.3.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
22-31Informations de copyright
Copyright © 2019. Published by Elsevier Inc.