ArticleJournal of the American Chemical Society2016
Photoinduced Electron Transfer Elicits a Change in the Static Dielectric Constant of a de Novo Designed Protein.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 28 citations in OpenAlex.
- De Novo Design of Proteins That Bind Naphthalenediimides, Powerful Photooxidants with Tunable Photophysical Properties.Journal of the American Chemical Society · 2025Article
- De novo design of four-helix bundle proteins to bind metalloporphyrin cofactors.Methods in enzymology · 2025Article
- Designed Rubredoxin miniature in a fully artificial electron chain triggered by visible light.Nature communications · 2023Article
- De novo metalloprotein design.Nature reviews. Chemistry · 2022Article
- Article
- Orientational Dependence of Cofacial Porphyrin-Quinone Electronic Interactions within the Strong Coupling Regime.The journal of physical chemistry. B · 2019Article
- Mean First-Passage Times in Biology.Israel journal of chemistry · 2016Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
We provide a direct measure of the change in effective dielectric constant (ε(S)) within a protein matrix after a photoinduced electron transfer (ET) reaction. A linked donor-bridge-acceptor molecule, PZn-Ph-NDI, consisting of a (porphinato)Zn donor (PZn), a phenyl bridge (Ph), and a naphthalene diimide acceptor (NDI), is shown to be a "meter" to indicate protein dielectric environment. We calibrated PZn-Ph-NDI ET dynamics as a function of solvent dielectric, and computationally de novo designed a protein SCPZnI3 to bind PZn-Ph-NDI in its interior. Mapping the protein ET dynamics onto the calibrated ET catalogue shows that SCPZnI3 undergoes a switch in the effective dielectric constant following photoinduced ET, from ε(S) ≈ 8 to ε(S) ≈ 3.
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Registered trials
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