Frustration Dynamics and Electron-Transfer Reorganization Energies in Wild-Type and Mutant Azurins.
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:
09 03 2022
09 03 2022
Historique:
pubmed:
17
2
2022
medline:
22
4
2022
entrez:
16
2
2022
Statut:
ppublish
Résumé
Long-range electron tunneling through metalloproteins is facilitated by evolutionary tuning of donor-acceptor electronic couplings, formal electrochemical potentials, and active-site reorganization energies. Although the minimal frustration of the folding landscape enables this tuning, residual frustration in the vicinity of the metallocofactor can allow conformational fluctuations required for protein function. We show here that the constrained copper site in wild-type azurin is governed by an intricate pattern of minimally frustrated local and distant interactions that together enable rapid electron flow to and from the protein. In contrast, sluggish electron transfer reactions (unfavorable reorganization energies) of active-site azurin variants are attributable to increased frustration near to as well as distant from the copper site, along with an exaggerated oxidation-state dependence of both minimally and highly frustrated interaction patterns.
Identifiants
pubmed: 35171591
doi: 10.1021/jacs.1c13454
pmc: PMC8915257
doi:
Substances chimiques
Azurin
12284-43-4
Copper
789U1901C5
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
4178-4185Subventions
Organisme : NIDDK NIH HHS
ID : R01 DK019038
Pays : United States
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