Artificial Diiron Enzymes with a de Novo Designed Four-Helix Bundle Structure (684 views)
Eur J Inorg Chem (ISSN: 1434-1948, 1099-0682e), 2015; 2015(21): 3371-3390.
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Paper type: Journal Article,
Impact factor: 2.686, 5-year impact factor: 2.68
Url: Not available.
Keywords: Df Models, Enzyme Mimics, Helical Structures, Iron, Metalloenzymes, Protein Design,
Affiliations:
*** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, Via Cintia, Naples, Italy
IBB, CNR, Via Mezzocannone 16, Naples, Italy
Department of Structural and Functional Biology, University of Naples Federico II, Via Cintia, Naples, Italy
Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, San Francisco, CA, United States
References:
Not available.
Eur J Inorg Chem (ISSN: 1434-1948, 1099-0682e), 2015; 2015(21): 3371-3390.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.686, 5-year impact factor: 2.68
Url: Not available.
Keywords: Df Models, Enzyme Mimics, Helical Structures, Iron, Metalloenzymes, Protein Design,
Affiliations:
*** IBB - CNR ***
Department of Chemical Sciences, University of Naples Federico II, Via Cintia, Naples, Italy
IBB, CNR, Via Mezzocannone 16, Naples, Italy
Department of Structural and Functional Biology, University of Naples Federico II, Via Cintia, Naples, Italy
Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, San Francisco, CA, United States
References:
Not available.
Artificial Diiron Enzymes with a de Novo Designed Four-Helix Bundle Structure
A single polypeptide chain may provide an astronomical number of conformers. Nature selected only a trivial number of them through evolution, composing an alphabet of scaffolds, that can afford the complete set of chemical reactions needed to support life. These structural templates are so stable that they allow several mutations without disruption of the global folding, even having the ability to bind several exogenous cofactors. With this perspective, metal cofactors play a crucial role in the regulation and catalysis of several processes. Nature is able to modulate the chemistry of metals, adopting only a few ligands and slightly different geometries. Several scaffolds and metal-binding motifs are representing the focus of intense interest in the literature. This review discusses the widespread four-helix bundle fold, adopted as a scaffold for metal binding sites in the context of de novo protein design to obtain basic biochemical components for biosensing or catalysis. In particular, we describe the rational refinement of structure/function in diiron-oxo protein models from the due ferri (DF) family. The DF proteins were developed by us through an iterative process of design and rigorous characterization, which has allowed a shift from structural to functional models. The examples reported herein demonstrate the importance of the synergic application of de novo design methods as well as spectroscopic and structural characterization to optimize the catalytic performance of artificial enzymes. The de novo design of nature-inspired four-helix bundle metalloproteins is discussed. Special attention is given to the rational refinement of structure/function in diiron-oxo protein models from the due ferri family, which has allowed a shift from structural to functional models. Copyright © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
A single polypeptide chain may provide an astronomical number of conformers. Nature selected only a trivial number of them through evolution, composing an alphabet of scaffolds, that can afford the complete set of chemical reactions needed to support life. These structural templates are so stable that they allow several mutations without disruption of the global folding, even having the ability to bind several exogenous cofactors. With this perspective, metal cofactors play a crucial role in the regulation and catalysis of several processes. Nature is able to modulate the chemistry of metals, adopting only a few ligands and slightly different geometries. Several scaffolds and metal-binding motifs are representing the focus of intense interest in the literature. This review discusses the widespread four-helix bundle fold, adopted as a scaffold for metal binding sites in the context of de novo protein design to obtain basic biochemical components for biosensing or catalysis. In particular, we describe the rational refinement of structure/function in diiron-oxo protein models from the due ferri (DF) family. The DF proteins were developed by us through an iterative process of design and rigorous characterization, which has allowed a shift from structural to functional models. The examples reported herein demonstrate the importance of the synergic application of de novo design methods as well as spectroscopic and structural characterization to optimize the catalytic performance of artificial enzymes. The de novo design of nature-inspired four-helix bundle metalloproteins is discussed. Special attention is given to the rational refinement of structure/function in diiron-oxo protein models from the due ferri family, which has allowed a shift from structural to functional models. Copyright © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Artificial Diiron Enzymes with a de Novo Designed Four-Helix Bundle Structure
| ▼ Biomolecular NMR: structural studies of proteins and peptides and drug discovery applications |
| ▼ Syntethic metalloproteins and peptides for biosensing applications |
Artificial Diiron Enzymes with a de Novo Designed Four-Helix Bundle Structure
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 3.929
View Export to BibTeX Export to EndNote
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Impact Factor: 2.572
View Export to BibTeX Export to EndNote
Chino M, Leone L, Zambrano G, Pirro F, D'Alonzo D, Firpo V, Aref D, Lista L, Maglio O, Nastri F, Lombardi A
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Impact Factor: 2.572
View Export to BibTeX Export to EndNote
Caserta G, Chino M, Firpo V, Zambrano G, Leone L, D'Alonzo D, Nastri F, Maglio O, Pavone V, Lombardi A
* Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design (299 views)
Chembiochem, 2018; 19: 1823-1826.
Impact Factor: 2.774
View Export to BibTeX Export to EndNote
Chino M, Leone L, Maglio O, D'Alonzo D, Pirro F, Pavone V, Nastri F, Lombardi A
* A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation (272 views) (PDF 171 views)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2017 Dec 4; 56(49): 15580-15583.
Impact Factor: 12.102
View Export to BibTeX Export to EndNote
Nastri F, Chino M, Maglio O, Bhagi-damodaran A, Lu Y, Lombardi A
* Design and engineering of artificial oxygen-activating metalloenzymes (230 views) (PDF 175 views)
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Impact Factor: 38.618
View Export to BibTeX Export to EndNote
Del Prete S, De Luca V, De Simone G, Supuran CT, Capasso C
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Impact Factor: 4.293
View Export to BibTeX Export to EndNote
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Impact Factor: 5.078
View Export to BibTeX Export to EndNote
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Impact Factor: 5.831
View Export to BibTeX Export to EndNote
Maglio O, Nastri F, Lombardi A, Ciferri A, Perico A
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Impact Factor: 5.927
View Export to BibTeX Export to EndNote
Nastri F, Lista L, Ringhieri P, Vitale R, Faiella M, Andreozzi C, Travascio P, Maglio O, Lombardi A, Pavone V
* A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity (574 views)
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Impact Factor: 5.925
View Export to BibTeX Export to EndNote
Grasso G, Pietropaolo A, Spoto G, Pappalardo G, Tundo GR, Ciaccio C, Coletta M, Rizzarelli E
* Copper(I) and Copper(II) Inhibit A beta Peptides Proteolysis by Insulin-Degrading Enzyme Differently: Implications for Metallostasis Alteration in Alzheimer's Disease (596 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Feb 25; 17(9): 2752-2762.
Impact Factor: 5.925
View Export to BibTeX Export to EndNote
La Mendola D, Magrì A, Campagna T, Campitiello MA, Raiola L, Isernia C, Hansson O, Bonomo RP, Rizzarelli E
* A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein (1189 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2010 Jun 1; 16(21): 6212-6223.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Diana D, Ziaco B, Scarabelli G, Pedone C, Colombo G, D'Andrea LD, Fattorusso R
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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
Diana D, Ziaco B, Colombo G, Scarabelli G, Romanelli A, Fedone C, Fattorusso R, D'Andrea LD
* Structural determinants of the unusual helix stability of a de novo engineered vascular endothelial growth factor (VEGF) mimicking peptide (488 views)
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Impact Factor: 5.454
View Export to BibTeX Export to EndNote
Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Micera G, Osz K, Pappalardo G, Rizzarelli E, Sanna D, Sovago I
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Impact Factor: 4.907
View Export to BibTeX Export to EndNote
Lahr SJ, Engel DE, Stayrook SE, Maglio O, North B, Geremia S, Lombardi A, Degrado WF
* Analysis and design of turns in α-helical hairpins (482 views)
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
* Artificial diiron proteins: From structure to function (518 views)
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
* Miniaturized heme proteins: crystal structure of Co(III)-mimochrome IV (393 views)
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
Saviano M, Improta R, Benedetti E, Carrozzini B, Cascarano GL, Didierjean C, Toniolo C, Crisma M
* Benzophenone photophore flexibility and proximity: Molecular and crystal-state structure of a Bpa-containing trichogin dodecapeptide analogue (393 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2004 Apr 2; 5(4): 541-544.
Impact Factor: 3.474
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 (543 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 (1187 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
Carotenuto L, Berisio R, Piccolo C, Vitagliano L, Zagari A
* Video observation of protein crystal growth in the advanced protein crystallization facility aboard the space shuttle mission STS-95 (393 views)
J Cryst Growth (ISSN: 0022-0248), 2001; 232(1-4): 481-488.
Impact Factor: 1.283
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De Luca S, Bruno G, Fattorusso R, Isernia C, Pedone C, Morelli G
New synthetic tools for peptide-tetraphenylporphyrin derivatives (330 views)
Int J Pept Res Ther (ISSN: 0929-5666, 1573-3149), 1998 Jul; 5(4): 269-276.
Impact Factor: 0.557
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Impellizzeri G, Pappalardo G, Purrello R, Rizzarelli E, Santoro AM
Synthesis, spectroscopic characterisation, and metal ion interaction of a new α-helical peptide (498 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1998; 4(9): 1791-1798.
Impact Factor: 5.153
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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 (677 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 (511 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 350-362.
Impact Factor: 4.828
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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 (9 views)
Angewandte Chemie International Edition, 2023/1/2; 62: e202211552-N/D.
Impact Factor: 16.823
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31 Records (30 excluding Abstracts).
Total impact factor: 191.566 (186.488 excluding Abstracts).
Total 5 year impact factor: 172.396 (167.318 excluding Abstracts).
Total impact factor: 191.566 (186.488 excluding Abstracts).
Total 5 year impact factor: 172.396 (167.318 excluding Abstracts).
684 views. Last view on Saturday 28 October 2023, 9:14:51
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