期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 56, 期 49, 页码 15580-15583出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201707637
关键词
bioinorganic chemistry; click chemistry; de novo protein design; diiron-oxo proteins; oxidoreductase
资金
- Scientific Research Department of Campania Region (STRAIN Project) [B25B0900000000]
Metalloproteins utilize O-2 as an oxidant, and they often achieve a 4-electron reduction without H2O2 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 (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 H2O2 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.
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