Mechanism of nitrite-dependent NO synthesis by human sulfite oxidase.
mitochondria
molybdenum cofactor
nitric oxide
nitrite reduction
sulfite oxidase
Journal
The Biochemical journal
ISSN: 1470-8728
Titre abrégé: Biochem J
Pays: England
ID NLM: 2984726R
Informations de publication
Date de publication:
28 06 2019
28 06 2019
Historique:
received:
26
02
2019
revised:
21
05
2019
accepted:
05
06
2019
pubmed:
7
6
2019
medline:
12
2
2020
entrez:
7
6
2019
Statut:
epublish
Résumé
In addition to nitric oxide (NO) synthases, molybdenum-dependent enzymes have been reported to reduce nitrite to produce NO. Here, we report the stoichiometric reduction in nitrite to NO by human sulfite oxidase (SO), a mitochondrial intermembrane space enzyme primarily involved in cysteine catabolism. Kinetic and spectroscopic studies provide evidence for direct nitrite coordination at the molybdenum center followed by an inner shell electron transfer mechanism. In the presence of the physiological electron acceptor cytochrome
Identifiants
pubmed: 31167903
pii: BCJ20190143
doi: 10.1042/BCJ20190143
doi:
Substances chimiques
Mitochondrial Proteins
0
Nitrites
0
Nitric Oxide
31C4KY9ESH
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
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
1805-1815Commentaires et corrections
Type : CommentIn
Informations de copyright
© 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.