Conformational control over proton-coupled electron transfer in metalloenzymes.
Journal
Nature reviews. Chemistry
ISSN: 2397-3358
Titre abrégé: Nat Rev Chem
Pays: England
ID NLM: 101703631
Informations de publication
Date de publication:
02 Sep 2024
02 Sep 2024
Historique:
accepted:
29
07
2024
medline:
3
9
2024
pubmed:
3
9
2024
entrez:
2
9
2024
Statut:
aheadofprint
Résumé
From the reduction of dinitrogen to the oxidation of water, the chemical transformations catalysed by metalloenzymes underlie global geochemical and biochemical cycles. These reactions represent some of the most kinetically and thermodynamically challenging processes known and require the complex choreography of the fundamental building blocks of nature, electrons and protons, to be carried out with utmost precision and accuracy. The rate-determining step of catalysis in many metalloenzymes consists of a protein structural rearrangement, suggesting that nature has evolved to leverage macroscopic changes in protein molecular structure to control subatomic changes in metallocofactor electronic structure. The proton-coupled electron transfer mechanisms operative in nitrogenase, photosystem II and ribonucleotide reductase exemplify this interplay between molecular and electronic structural control. We present the culmination of decades of study on each of these systems and clarify what is known regarding the interplay between structural changes and functional outcomes in these metalloenzyme linchpins.
Identifiants
pubmed: 39223400
doi: 10.1038/s41570-024-00646-7
pii: 10.1038/s41570-024-00646-7
doi:
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2024. Springer Nature Limited.
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