E
Enrico Monzani
Researcher at University of Catania
Publications - 6
Citations - 301
Enrico Monzani is an academic researcher from University of Catania. The author has contributed to research in topics: Substrate (chemistry) & Chemical stability. The author has an hindex of 3, co-authored 6 publications receiving 283 citations.
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Journal ArticleDOI
Tyrosinase Models. Synthesis, Structure, Catechol Oxidase Activity, and Phenol Monooxygenase Activity of a Dinuclear Copper Complex Derived from a Triamino Pentabenzimidazole Ligand.
Enrico Monzani,Luisa Quinti,Angelo Perotti,Luigi Casella,Michele Gullotti,Lucio Randaccio,Silvano Geremia,Giorgio Nardin,Paolo Faleschini,Giovanni Tabbì +9 more
TL;DR: Kinetic experiments show that [Cu(2)(L-55)](4+) is the most efficient catalyst (rate constant 140 M(-1) s(-1)), followed by [Cu (2)(LB5)]( 4+) (60 M(- 1) s (-1)), in this oxidation, while [ Cu(2(L-66)] (4+) undergoes an extremely fast stoichiometric phase followed by a slow and substrate-concentration-independent catalytic phase.
Journal ArticleDOI
Engineering and Prosthetic-Group Modification of Myoglobin: Peroxidase Activity, Chemical Stability and Unfolding Properties
TL;DR: The approach to enhance the peroxidase-like activity of Mb toward phenolic compounds by combining two different strategies of protein modification, i.e. active-site engineering and cofactor replacement is summarized.
Journal ArticleDOI
Biomimetic oxidation catalysis by iron (III) deuteroporpbyrin carrying a deca-L-alanine peptide chain
TL;DR: In this paper, the deuterohemin complex carrying a deca-L-alanine peptide residue covalently linked to one of the propionic acid side chain of the porphyrin has been synthesized and its catalytic behaviour in biomimetic oxidations has been investigated by kinetic measurements.
Journal ArticleDOI
Engineering and Prosthetic-Group Modification of Myoglobin: Peroxidase Activity, Chemical Stability and Unfolding Properties.
TL;DR: In this paper, an approach to enhance the peroxidase-like activity of myoglobin toward phenolic compounds by combining two different strategies of protein modification, i.e. active-site engineering and cofactor replacement, was presented.
Account / Revue Heme-peptide complexes as peroxidase models
TL;DR: Heme-peptide complexes can be used as model systems for peroxidases and four different approaches are described, linking a peptide residue to hemin or deuterohemin, with the aim of introducing substrate selectivity or stereoselectivity in the catalytic activity.