A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation(49 visite)(PDF pubblico53 visite) Chino M, Leone L, Maglio O, D'Alonzo D, Pirro F, Pavone V, Nastri F, Lombardi A
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic), 2017 Dec 4; 56(49): 15580-15583.
Tipo di articolo: Journal Article,
Impact factor: 12.102, Impact factor a 5 anni: 11.954
Url: Non disponibile.
Parole chiave: Bioinorganic Chemistry, Click Chemistry, De Novo Protein Design, Diiron-Oxo Proteins, Oxidoreductase,
Affiliazioni:
*** IBB - CNR *** Department of Chemical Sciences, University of Napoli "Federico II", Via Cintia, 80126, Napoli, Italy., IBB-National Research Council, Via Mezzocannone 16, 80134, Napoli, Italy.,
Riferimenti:
Non disponibile.
Metalloproteins utilize O2 as an oxidant, and they often achieve a 4-electron reduction without H2 O2 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 O2 has not been reported yet. We report the construction of a diiron-binding four-helix bundle, made up of two different covalently linked alpha2 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 H2 O2 in the oxidation of 4-aminophenol in the presence of O2 , 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.
39 Records (38 escludendo Abstract e Conferenze). Impact factor totale: 146.943 (144.061 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 164.402 (161.52 escludendo Abstract e Conferenze).
ibb.cnr.it