Electrochemical and Structural Study of the Buried Tryptophan in Azurin: Effects of Hydration and Polarity on the Redox Potential of W48.
Journal
The journal of physical chemistry. B
ISSN: 1520-5207
Titre abrégé: J Phys Chem B
Pays: United States
ID NLM: 101157530
Informations de publication
Date de publication:
12 01 2023
12 01 2023
Historique:
pmc-release:
21
12
2023
pubmed:
22
12
2022
medline:
14
1
2023
entrez:
21
12
2022
Statut:
ppublish
Résumé
Tryptophan serves as an important redox-active amino acid in mediating electron transfer and mitigating oxidative damage in proteins. We previously showed a difference in electrochemical potentials for two tryptophan residues in azurin with distinct hydrogen-bonding environments. Here, we test whether reducing the side chain bulk at position Phe110 to Leu, Ser, or Ala impacts the electrochemical potentials (
Identifiants
pubmed: 36542812
doi: 10.1021/acs.jpcb.2c06677
pmc: PMC9841983
doi:
Substances chimiques
Azurin
12284-43-4
Tryptophan
8DUH1N11BX
Hydrogen
7YNJ3PO35Z
Water
059QF0KO0R
Types de publication
Journal Article
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
133-143Références
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