The energetics and evolution of oxidoreductases in deep time.
electrons
energy metabolism
enzymes and coenzymes oxidation-reduction oxidoreductases proteins
Journal
Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181
Informations de publication
Date de publication:
19 Aug 2023
19 Aug 2023
Historique:
received:
16
05
2023
accepted:
06
07
2023
medline:
19
8
2023
pubmed:
19
8
2023
entrez:
19
8
2023
Statut:
aheadofprint
Résumé
The core metabolic reactions of life drive electrons through a class of redox protein enzymes, the oxidoreductases. The energetics of electron flow is determined by the redox potentials of organic and inorganic cofactors as tuned by the protein environment. Understanding how protein structure affects oxidation-reduction energetics is crucial for studying metabolism, creating bioelectronic systems, and tracing the history of biological energy utilization on Earth. We constructed ProtReDox (https://protein-redox-potential.web.app), a manually curated database of experimentally determined redox potentials. With over 500 measurements, we can begin to identify how proteins modulate oxidation-reduction energetics across the tree of life. By mapping redox potentials onto networks of oxidoreductase fold evolution, we can infer the evolution of electron transfer energetics over deep time. ProtReDox is designed to include user-contributed submissions with the intention of making it a valuable resource for researchers in this field.
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NASA Astrobiology Institute
ID : 80NSSC18M0093
Organisme : U.S. National Science Foundation
ID : CHE-2201279
Organisme : U.S. National Science Foundation
ID : MCB-2025200
Organisme : NIH IRACDA Postdoctoral Fellowship Program
ID : K12GM093854
Organisme : RISE program at Rutgers University
Informations de copyright
© 2023 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals LLC.
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