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• W2766348889 endingPage "15583" @default.
• W2766348889 startingPage "15580" @default.
• W2766348889 abstract "Abstract Metalloproteins utilize O 2 as an oxidant, and they often achieve a 4‐electron reduction without H 2 O 2 or oxygen radical release. Several proteins have been designed to catalyze one or two‐electron oxidative chemistry, but the de novo design of a protein that catalyzes the net 4‐electron reduction of O 2 has not been reported yet. We report the construction of a diiron‐binding four‐helix bundle, made up of two different covalently linked α 2 monomers, through click chemistry. Surprisingly, the prototype protein, DF‐C1, showed a large divergence in its reactivity from earlier DFs (DF: due ferri, two iron). DFs release the quinone imine and free H 2 O 2 in the oxidation of 4‐aminophenol in the presence of O 2 , whereas Fe III ‐DF‐C1 sequesters the quinone imine into the active site, and catalyzes inside the scaffold an oxidative coupling between oxidized and reduced 4‐aminophenol. The asymmetry of the scaffold allowed a fine‐engineering of the substrate binding pocket, that ensures selectivity." @default.
• W2766348889 created "2017-11-10" @default.
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• W2766348889 date "2017-11-14" @default.
• W2766348889 modified "2023-10-10" @default.
• W2766348889 title "A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation" @default.
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• W2766348889 doi "https://doi.org/10.1002/anie.201707637" @default.
• W2766348889 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29053213" @default.
• W2766348889 hasPublicationYear "2017" @default.
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