In:
Angewandte Chemie, Wiley, Vol. 129, No. 49 ( 2017-12-04), p. 15786-15786
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.
Type of Medium:
Online Resource
ISSN:
0044-8249
,
1521-3757
DOI:
10.1002/ange.v129.49
DOI:
10.1002/ange.201707637
Language:
English
Publisher:
Wiley
Publication Date:
2017
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