A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity (787 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Apr; 17(16): 4444-4453.
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Paper type: Journal Article,
Impact factor: 5.925, 5-year impact factor: 5.866
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79953713973&partnerID=40&md5=39abedcde07a73f0f31071229caf1492
Keywords: Bioinorganic Chemistry, Heme Proteins, Michaelis-Menten Kinetics, Peroxidase Activity, Protein Design, Biochemistry, Biomimetics, Catalyst Activity, Enzymes, Hydrogen Peroxide, Oxidation, Peptides, Phenols, Porphyrins, Enzyme Activity, Horseradish Peroxidase, Amino Acid Sequence, Article, Chemical Model, Chemical Structure, Metabolism, Nuclear Magnetic Resonance, Molecular Structure, Biomolecular,
Affiliations:
*** IBB - CNR ***
Department of Chemistry, Complesso Universitario Monte S. Angelo, University of Naples Federico II, Via Cintia, 80126 Naples, Italy
IBB, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
References:
Not available.
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Apr; 17(16): 4444-4453.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.925, 5-year impact factor: 5.866
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79953713973&partnerID=40&md5=39abedcde07a73f0f31071229caf1492
Keywords: Bioinorganic Chemistry, Heme Proteins, Michaelis-Menten Kinetics, Peroxidase Activity, Protein Design, Biochemistry, Biomimetics, Catalyst Activity, Enzymes, Hydrogen Peroxide, Oxidation, Peptides, Phenols, Porphyrins, Enzyme Activity, Horseradish Peroxidase, Amino Acid Sequence, Article, Chemical Model, Chemical Structure, Metabolism, Nuclear Magnetic Resonance, Molecular Structure, Biomolecular,
Affiliations:
*** IBB - CNR ***
Department of Chemistry, Complesso Universitario Monte S. Angelo, University of Naples Federico II, Via Cintia, 80126 Naples, Italy
IBB, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
References:
Not available.
A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity
Mimicking enzymes with alternative molecules represents an important objective in synthetic biology, aimed to obtain new chemical entities for specific applications. This objective is hampered by the large size and complexity of enzymes. The manipulation of their structures often leads to a reduction of enzyme activity. Herein, we describe the spectroscopic and functional characterization of Fe(III)-mimochrome VI, a 3.5 kDa synthetic hemeprotein model, which displays a peroxidase-like catalytic activity. By the use of hydrogen peroxide, Fe(III)-mimochrome VI efficiently catalyzes the oxidation of several substrates, with a typical Michaelis-Menten mechanism and with several multiple turnovers. The catalytic efficiency of Fe(III)-mimochrome VI in the oxidation of 2,2'-azino-di(3-ethyl-benzothiazoline-6-sulfonic acid (ABTS) and guaiacol (k(cat)/K(m)=4417 and 870 mM(-1)s(-1), respectively) is comparable to that of native horseradish peroxidase (HRP, k(cat)/K(m)=5125 and 500 mM(-1)s(-1), respectively). Fe(III)-mimochrome VI also converts phenol to 4- and 2-nitrophenol in the presence of NO(2)(-) and H(2)O(2) in high yields. These results demonstrate that small synthetic peptides can impart high enzyme activities to metal cofactors, and anticipate the possibility of constructing new biocatalysts tailored to specific functions.
Mimicking enzymes with alternative molecules represents an important objective in synthetic biology, aimed to obtain new chemical entities for specific applications. This objective is hampered by the large size and complexity of enzymes. The manipulation of their structures often leads to a reduction of enzyme activity. Herein, we describe the spectroscopic and functional characterization of Fe(III)-mimochrome VI, a 3.5 kDa synthetic hemeprotein model, which displays a peroxidase-like catalytic activity. By the use of hydrogen peroxide, Fe(III)-mimochrome VI efficiently catalyzes the oxidation of several substrates, with a typical Michaelis-Menten mechanism and with several multiple turnovers. The catalytic efficiency of Fe(III)-mimochrome VI in the oxidation of 2,2'-azino-di(3-ethyl-benzothiazoline-6-sulfonic acid (ABTS) and guaiacol (k(cat)/K(m)=4417 and 870 mM(-1)s(-1), respectively) is comparable to that of native horseradish peroxidase (HRP, k(cat)/K(m)=5125 and 500 mM(-1)s(-1), respectively). Fe(III)-mimochrome VI also converts phenol to 4- and 2-nitrophenol in the presence of NO(2)(-) and H(2)O(2) in high yields. These results demonstrate that small synthetic peptides can impart high enzyme activities to metal cofactors, and anticipate the possibility of constructing new biocatalysts tailored to specific functions.
A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity
| ▼ Syntethic metalloproteins and peptides for biosensing applications |
A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity
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Impact Factor: 13.324
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 5.831
View Export to BibTeX Export to EndNote
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Impact Factor: 5.927
View Export to BibTeX Export to EndNote
Kállay C, Turi I, Timári S, Nagy Z, Sanna D, Pappalardo G, De Bona P, Rizzarelli E, Sóvágó I
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Impact Factor: 1.532
View Export to BibTeX Export to EndNote
Diana D, Ziaco B, Scarabelli G, Pedone C, Colombo G, D'Andrea LD, Fattorusso R
* Structural analysis of a helical peptide unfolding pathway (600 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2010 May 10; 16(18): 5400-5407.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Lahr SJ, Engel DE, Stayrook SE, Maglio O, North B, Geremia S, Lombardi A, Degrado WF
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J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2005; 346(5): 1441-1454.
Impact Factor: 5.229
View Export to BibTeX Export to EndNote
Calhoun JR, Nastri F, Maglio O, Pavone V, Lombardi A, Degrado WF
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Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2005; 80(2-3): 264-278.
Impact Factor: 2.545
View Export to BibTeX Export to EndNote
Di Costanzo L, Geremia S, Randaccio L, Nastri F, Maglio O, Lombardi A, Pavone V
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J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257print), 2004 Dec; 9(8): 1017-1027.
Impact Factor: 3.3
View Export to BibTeX Export to EndNote
Lombardi A, Nastri F, Marasco D, Maglio O, De Sanctis G, Sinibaldi F, Santucci R, Coletta M, Pavone V
* Design of a new mimochrome with unique topology (591 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2003 Nov 21; 9(22): 5643-5654.
Impact Factor: 4.353
View Export to BibTeX Export to EndNote
Main ERG, Xiong Y, Cocco MJ, D'Andrea LD, Regan L
* Design of stable α-helical arrays from an idealized TPR motif (1496 views)
Structure (ISSN: 0969-2126, 1878-4186, 0969-2126linking), 2003; 11(5): 497-508.
Impact Factor: 5.993
View Export to BibTeX Export to EndNote
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 (772 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 (600 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
Pacelli R, Taira J, Cook JA, Wink DA, Krishna MC
Hydroxyurea reacts with heme proteins to generate nitric oxide [6] (454 views)
Lancet (ISSN: 0140-6736), 1996 Mar 30; 347(9005): 900-900.
Impact Factor: 16.135
View Export to BibTeX Export to EndNote
Pirro F, La Gatta S, Arrigoni F, Famulari A, Maglio O, Vecchio PD, Chiesa M, De Gioia L, Bertini L, Chino M, Nastri F, Lombardi A
* A De Novo‐Designed Type 3 Copper Protein Tunes Catechol Substrate Recognition and Reactivity (89 views)
Angewandte Chemie International Edition, 2023/1/2; 62: e202211552-N/D.
Impact Factor: 16.823
View Export to BibTeX Export to EndNote
20 Records (19 excluding Abstracts).
Total impact factor: 132.154 (116.019 excluding Abstracts).
Total 5 year impact factor: 119.524 (95.323 excluding Abstracts).
Total impact factor: 132.154 (116.019 excluding Abstracts).
Total 5 year impact factor: 119.524 (95.323 excluding Abstracts).
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