Protein engineering a PhotoRNR chimera based on a unifying evolutionary apparatus among the natural classes of ribonucleotide reductases.

10-stranded αβ barrel chimeric enzyme proton-coupled electron transfer radical transport ribonucleotide reductase

Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
30 Apr 2024
Historique:
medline: 23 4 2024
pubmed: 23 4 2024
entrez: 22 4 2024
Statut: ppublish

Résumé

Ribonucleotide reductases (RNRs) are essential enzymes that catalyze the de novo transformation of nucleoside 5'-di(tri)phosphates [ND(T)Ps, where N is A, U, C, or G] to their corresponding deoxynucleotides. Despite the diversity of factors required for function and the low sequence conservation across RNRs, a unifying apparatus consolidating RNR activity is explored. We combine aspects of the protein subunit simplicity of class II RNR with a modified version of

Identifiants

pubmed: 38648489
doi: 10.1073/pnas.2317291121
doi:

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

e2317291121

Subventions

Organisme : HHS | National Institutes of Health (NIH)
ID : GM047274

Déclaration de conflit d'intérêts

Competing interests statement:The authors declare no competing interest.

Auteurs

David Y Song (DY)

Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138.

JoAnne Stubbe (J)

Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138.

Daniel G Nocera (DG)

Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138.

Classifications MeSH