Charge Transfer between [4Fe4S] Proteins and DNA Is Unidirectional: Implications for Biomolecular Signaling.
Journal
Chem
ISSN: 2451-9294
Titre abrégé: Chem
Pays: United States
ID NLM: 101688902
Informations de publication
Date de publication:
10 Jan 2019
10 Jan 2019
Historique:
entrez:
5
2
2019
pubmed:
5
2
2019
medline:
5
2
2019
Statut:
ppublish
Résumé
Recent experiments suggest that DNA-mediated charge transport might enable signaling between the [4Fe4S] clusters in the C-terminal domains of human DNA primase and polymerase α, as well as the signaling between other replication and repair high-potential [4Fe4S] proteins. Our theoretical study demonstrates that the redox signaling cannot be accomplished exclusively by DNA-mediated charge transport because part of the charge transfer chain has an unfavorable free energy profile. We show that hole or excess electron transfer between a [4Fe4S] cluster and a nucleic acid duplex through a protein medium can occur within microseconds in one direction, while it is kinetically hindered in the opposite direction. We present a set of signaling mechanisms that may occur with the assistance of oxidants or reductants, using the allowed charge transfer processes. These mechanisms would enable the coordinated action of [4Fe4S] proteins on DNA, engaging the [4Fe4S] oxidation state dependence of the protein-DNA binding affinity.
Identifiants
pubmed: 30714018
doi: 10.1016/j.chempr.2018.09.026
pmc: PMC6350243
mid: NIHMS1508891
doi:
Types de publication
Journal Article
Langues
eng
Pagination
122-137Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM048043
Pays : United States
Commentaires et corrections
Type : ErratumIn
Déclaration de conflit d'intérêts
Declaration of Interests The authors declare no competing interests.
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