Artificial Diiron Enzymes with a de Novo Designed Four-Helix Bundle Structure (596 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
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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
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Chino, M., Leone, L., Liguori, D., Maglio, O., Nastri, F., Pavone, V., Lombardi, A., unpublished results, manuscript in preparationUR - http://www.scopus.com/inward/record.url?eid=2-s2.0-84938197232&partnerID=40&md5=b2f625328bfe5b8813790bb9de5f0690
Eur J Inorg Chem (ISSN: 1434-1948, 1099-0682e), 2015; 2015(21): 3371-3390.
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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
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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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Impact Factor: 0
View Export to BibTeX Export to EndNote
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* Highly Selective Indole Oxidation Catalyzed by a Mn-Containing Artificial Mini-Enzyme (2 views) (PDF 3 views)
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Impact Factor: 13.7
View Export to BibTeX Export to EndNote
Mercurio FA, Di Natale C, Pirone L, Vincenzi M, Marasco D, De Luca S, Pedone EM, Leone M
* Exploring the ability of cyclic peptides to target SAM domains: a computational and experimental study (266 views)
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Impact Factor: 2.641
View Export to BibTeX Export to EndNote
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* The zinc - but not cadmium - containing zeta-carbonic from the diatom Thalassiosira weissflogii is potently activated by amines and amino acids (284 views)
Bioorg Chem (ISSN: 1090-2120electronic, 0045-2068linking), 2018 Oct; 80: 261-265.
Impact Factor: 3.929
View Export to BibTeX Export to EndNote
Chino M, Zhang SQ, Pirro F, Leone L, Maglio O, Lombardi A, Degrado WF
* Spectroscopic and metal binding properties of a de novo metalloprotein binding a tetrazinc cluster (347 views)
Biopolymers (ISSN: 1097-0282electronic, 0006-3525linking, 0006-3525print), 2018 Sep 11; 109(10): e23339-e23339.
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
* Oxidation catalysis by iron and manganese porphyrins within enzyme-like cages (241 views)
Biopolymers (ISSN: 0006-3525linking, 0006-3525print, 1097-0282electronic), 2018 Aug; 109(10): e23107-e23107.
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 (266 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 (246 views) (PDF 169 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 (224 views) (PDF 171 views)
Chem Soc Rev (ISSN: 0306-0012, 1460-4744), 2016 Sep 21; 45(18): 5020-5054.
Impact Factor: 38.618
View Export to BibTeX Export to EndNote
Del Prete S, De Luca V, De Simone G, Supuran CT, Capasso C
* Cloning, expression and purification of the complete domain of the eta-carbonic anhydrase from Plasmodium falciparum (353 views)
J Enzym Inhib Med Ch (ISSN: 1475-6366, 1475-6374electronic, 1475-6366linking), 2016 Jun; 31(sup4): 54-59.
Impact Factor: 4.293
View Export to BibTeX Export to EndNote
Pannuzzo M, Raudino A, Milardi D, La Rosa C, Karttunen M
* α-Helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes (753 views)
Sci Rep (ISSN: 2045-2322, 2045-2322electronic, 2045-2322linking), 2013; 3: N/D-N/D.
Impact Factor: 5.078
View Export to BibTeX Export to EndNote
Faiella M, Maglio O, Nastri F, Lombardi A, Lista L, Hagen WR, Pavone V
* De Novo Design, Synthesis and Characterisation of MP3, A New Catalytic Four-Helix Bundle Hemeprotein (479 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2012 Dec 7; 18(50): 15960-15971.
Impact Factor: 5.831
View Export to BibTeX Export to EndNote
Maglio O, Nastri F, Lombardi A, Ciferri A, Perico A
* Structural and Functional Aspects of Metal Binding Sites in Natural and Designed Metalloproteins (540 views)
Ionic Interactions In Nat And Synthetic Macromolecules John Wiley And Sons (ISSN: 9780-4705), 2012; N/D: 361-450.
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 (450 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Apr; 17(16): 4444-4453.
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 (576 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 (1135 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
* Structural analysis of a helical peptide unfolding pathway (507 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
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 (470 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2008; 14(14): 4164-4166.
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
* Environmental effects on a prion's helix II domain: copper(II) and membrane interactions with PrP180-193 and its analogues (432 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2005 Dec 23; 12(2): 537-547.
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 (472 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 (490 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 (379 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 (386 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2004 Apr 2; 5(4): 541-544.
Impact Factor: 3.474
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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 (534 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2003 Nov 21; 9(22): 5643-5654.
Impact Factor: 4.353
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Main ERG, Xiong Y, Cocco MJ, D'Andrea LD, Regan L
* Design of stable α-helical arrays from an idealized TPR motif (939 views)
Structure (ISSN: 0969-2126, 1878-4186, 0969-2126linking), 2003; 11(5): 497-508.
Impact Factor: 5.993
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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 (384 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 (326 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 (491 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 (615 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 (489 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 (6 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).
596 views. Last view on Tuesday 23 May 2023, 6:52:38
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