Structural snapshots of nitrosoglutathione binding and reactivity underlying S-nitrosylation of photosynthetic GAPDH.
And S-Nitrosylation
Chlamydomonas
Cysteine
Nitrosoglutathione
Photosynthetic GAPDH
Journal
Redox biology
ISSN: 2213-2317
Titre abrégé: Redox Biol
Pays: Netherlands
ID NLM: 101605639
Informations de publication
Date de publication:
08 2022
08 2022
Historique:
received:
15
06
2022
accepted:
25
06
2022
pubmed:
7
7
2022
medline:
14
7
2022
entrez:
6
7
2022
Statut:
ppublish
Résumé
S-nitrosylation is a redox post-translational modification widely recognized to play an important role in cellular signaling as it can modulate protein function and conformation. At the physiological level, nitrosoglutathione (GSNO) is considered the major physiological NO-releasing compound due to its ability to transfer the NO moiety to protein thiols but the structural determinants regulating its redox specificity are not fully elucidated. In this study, we employed photosynthetic glyceraldehyde-3-phosphate dehydrogenase from Chlamydomonas reinhardtii (CrGAPA) to investigate the molecular mechanisms underlying GSNO-dependent thiol oxidation. We first observed that GSNO causes reversible enzyme inhibition by inducing S-nitrosylation. While the cofactor NADP
Identifiants
pubmed: 35793584
pii: S2213-2317(22)00159-8
doi: 10.1016/j.redox.2022.102387
pmc: PMC9287727
pii:
doi:
Substances chimiques
Sulfhydryl Compounds
0
Nitric Oxide
31C4KY9ESH
NADP
53-59-8
S-Nitrosoglutathione
57564-91-7
Glyceraldehyde-3-Phosphate Dehydrogenases
EC 1.2.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
102387Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.
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