Chemical Communications · 2018 · 30 citations · 19 references
Natural SciencesBiochemistryChemistryCatalysisProtein EngineeringRedox BiochemistryBioinorganic ChemistryCatalytic MechanismsMetal-ligand BondingReactive Oxygen SpeciesRedox ChemistryRedox EnzymesArtificial Metalloenzyme DesignArtificial MetalloenzymesCatalytic ActivityCopper BiochemistryCopper ProteinsMetal-binding ProteinsMetalloenzyme EngineeringReactive Oxygen Species Generation
The catalytic redox activity of Cu(ii) bound to the motif NH2-Xxx-Zzz-His (ATCUN) with ascorbate and H2O2/O2 is very low and can be stopped via Cu(i)-chelation. This impacts its application as an artificial Cu-enzyme to degrade biomolecules via production of reactive oxygen species in a Cu(i)-chelator rich environment like the cytosol.
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Hydroperoxide metabolism in mammalian organs.
B Chance, Helmut Sies, A Boveris · Physiological Reviews · 1979 · 5.8K citations
Specific structure–stability relations in metallopeptides
Henryk Kozłowski, Wojciech Bal, Marcin Dyba et al. · Coordination Chemistry Reviews · 1999 · 445 citations