An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization (586 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2015 Apr 22; 13(17): 4859-4868.
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Paper type: Journal Article,
Impact factor: 3.559, 5-year impact factor: 3.367
Url: http://pubs.rsc.org/en/content/articlepdf/2015/ob/c5ob00257e
Keywords: 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,
Affiliations:
*** 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
References:
Not available.
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2015 Apr 22; 13(17): 4859-4868.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.559, 5-year impact factor: 3.367
Url: http://pubs.rsc.org/en/content/articlepdf/2015/ob/c5ob00257e
Keywords: 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,
Affiliations:
*** 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
References:
Not available.
An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization
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.
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.
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
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Nastri F, Lombardi A, Morelli G, Maglio O, D'Auria G, Pedone C, Pavone V
Hemoprotein models based on a covalent helix-heme-helix sandwich: 1. Design, synthesis, and characterization (773 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 340-349.
Impact Factor: 4.828
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D'Auria G, Maglio O, Nastri F, Lombardi A, Mazzeo M, Morelli G, Paolillo L, Pedone C, Pavone V
Hemoprotein models based on a covalent helix-heme-helix sandwich: 2. Structural characterization of Co(III) mimochrome I Δ and Λ isomers (603 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 350-362.
Impact Factor: 4.828
View Export to BibTeX Export to EndNote
Hemoprotein models based on a covalent helix-heme-helix sandwich: 1. Design, synthesis, and characterization (773 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 340-349.
Impact Factor: 4.828
View Export to BibTeX Export to EndNote
D'Auria G, Maglio O, Nastri F, Lombardi A, Mazzeo M, Morelli G, Paolillo L, Pedone C, Pavone V
Hemoprotein models based on a covalent helix-heme-helix sandwich: 2. Structural characterization of Co(III) mimochrome I Δ and Λ isomers (603 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 350-362.
Impact Factor: 4.828
View Export to BibTeX Export to EndNote
2 Records (2 excluding Abstracts).
Total impact factor: 9.656 (9.656 excluding Abstracts).
Total 5 year impact factor: 10.244 (10.244 excluding Abstracts).
Total impact factor: 9.656 (9.656 excluding Abstracts).
Total 5 year impact factor: 10.244 (10.244 excluding Abstracts).
586 views. Last view on Sunday 13 October 2024, 15:13:43
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