Metal/ADP Complexes Promote Phosphorylation of Ribonucleotides.


Journal

Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056

Informations de publication

Date de publication:
04 10 2023
Historique:
medline: 5 10 2023
pubmed: 26 9 2023
entrez: 26 9 2023
Statut: ppublish

Résumé

Under enzyme catalysis, adenosine triphosphate (ATP) transfers a phosphoryl group to canonical ribonucleotide diphosphates (NDPs) to form ribonucleotide triphosphates (NTPs), the direct biosynthetic precursors to RNA. However, it remains unclear whether the phosphorylation of NDPs could have occurred in water before enzymes existed and why an adenosine derivative, rather than another canonical NTP, typically performs this function. Here, we show that adenosine diphosphate (ADP) in the presence of Fe

Identifiants

pubmed: 37750669
doi: 10.1021/jacs.3c08047
doi:

Substances chimiques

Ribonucleotides 0
Coordination Complexes 0
N,N-di-n-propylserotonin 36288-75-2
Adenosine Triphosphate 8L70Q75FXE
Adenosine Diphosphate 61D2G4IYVH
Adenosine K72T3FS567
Water 059QF0KO0R

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

21630-21637

Auteurs

Emilie Werner (E)

ISIS UMR 7006, University of Strasbourg, CNRS, 67000 Strasbourg, France.

Silvana Pinna (S)

ISIS UMR 7006, University of Strasbourg, CNRS, 67000 Strasbourg, France.

Robert J Mayer (RJ)

ISIS UMR 7006, University of Strasbourg, CNRS, 67000 Strasbourg, France.

Joseph Moran (J)

ISIS UMR 7006, University of Strasbourg, CNRS, 67000 Strasbourg, France.
Institut Universitaire de France (IUF), 75005 Paris, France.
Department of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, Ontario K1N 6N5, Canada.

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Classifications MeSH