An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization
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An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization (235 visite)

Vitale R, Lista L, Cerrone C, Caserta G, Chino M, Maglio O, Nastri F, Pavone V, Lombardi A

ORG BIOMOL CHEM (ISSN: 1477-0520), 2015 Apr 22; 13(17): 4859-4868.



Tipo di articolo: Journal Article,

Impact factor: 3.559, Impact factor a 5 anni: 3.367

Url: http://pubs.rsc.org/en/content/articlepdf/2015/ob/c5ob00257e

Parole chiave: Magnetic Circular-Dichroism; De-Novo Design; Horseradish-Peroxidase; Helix Sandwich; Cytochrome-C; Miniaturized Hemoproteins; Molecular-Dynamics; Aqueous-Solution; Mimochrome Vi; Peptide, Amino Acids, Enzyme Activity, Porphyrins, Rational Functions, Scaffolds, Scaffolds (biology), Amino Acid Substitution, Artificial Heme Enzymes, Asymmetric System, Enhanced Catalytic Activity, Functional Screening, Peroxidase Activities, Peroxidase-Like Activities, Structural Characterization, Catalyst Activity,

Affiliazioni:

*** IBB - CNR ***
Department of Chemical Sciences, University of Naples, "Federico II", Via Cintia, 80126 Naples, Italy.
Collège de France, 11 place Marcelin Berthelot, 75231 Paris Cedex 05, France
IBB, CNR, Via Mezzocannone 16, 80134 Naples, Italy
IMAST Scarl, Piazza Bovio 22, 80133 Naples, Italy


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Synthetic proteins represent useful tools for reproducing metalloprotein functions in minimal, well-defined scaffolds. Herein, we describe the rational refinement of function into heme-protein models from the Mimochrome family. Originally designed to mimic the bis-His cytochrome b, the Mimochrome structure was modified to introduce a peroxidase-like activity, by creating a distal cavity on the heme. The success with the first asymmetric system, Mimochrome VI (MC6), gave the opportunity to explore further modifications in order to improve the catalytic activity. Starting from ferric MC6, single amino acid substitutions were introduced in the peptide chains to obtain four compounds, which were screened for peroxidase activity. The detailed structural and functional analysis of the best analogue, FeIII-E2L(TD)-MC6, indicates that an arginine residue in proximity to the heme-distal site could assist with catalysis by favoring the formation of the intermediate "compound I", thus mimicking R38 in HRP. This result highlights the potential of using small scaffolds for exploring the main factors that tune the heme-protein activity, and for programming new desired functions. This journal is © The Royal Society of Chemistry 2015.
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5 Records (4 escludendo Abstract e Conferenze).
Impact factor totale: 14.167 (14.167 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 15.432 (15.432 escludendo Abstract e Conferenze).







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