Spectroscopic and metal-binding properties of DF3: an artificial protein able to accommodate different metal ions (429 views)
J Biol Inorg Chem (ISSN: 1432-1327electronic, 0949-8257linking, 0949-8257print), 2010 Jun; 15(5): 717-728.
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Paper type: Journal Article, Research Support, N. I. H. , Extramural, Non-U. S. Gov'T,
Impact factor: 3.287, 5-year impact factor: 3.323
Url: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2915772/
Keywords: Di-Iron-Oxo Proteins, Four-Helix Bundle, Metalloprotein Models, Thermodynamic Stability, Spectroscopic Characterization, Azides, Chemistry, Binding Sites, Cobalt, Metabolism, Crystallography, X-Ray, Electron Spin Resonance Spectroscopy, Manganese, Chemical Synthesis, Molecular, Protein Stability, Spectrophotometry, Ultraviolet, Spectrum Analysis, Raman,
Affiliations:
*** IBB - CNR ***
Department of Chemistry, University of Naples "Federico II", Italy.,
References:
Not available.
J Biol Inorg Chem (ISSN: 1432-1327electronic, 0949-8257linking, 0949-8257print), 2010 Jun; 15(5): 717-728.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, N. I. H. , Extramural, Non-U. S. Gov'T,
Impact factor: 3.287, 5-year impact factor: 3.323
Url: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2915772/
Keywords: Di-Iron-Oxo Proteins, Four-Helix Bundle, Metalloprotein Models, Thermodynamic Stability, Spectroscopic Characterization, Azides, Chemistry, Binding Sites, Cobalt, Metabolism, Crystallography, X-Ray, Electron Spin Resonance Spectroscopy, Manganese, Chemical Synthesis, Molecular, Protein Stability, Spectrophotometry, Ultraviolet, Spectrum Analysis, Raman,
Affiliations:
*** IBB - CNR ***
Department of Chemistry, University of Naples "Federico II", Italy.,
References:
Not available.
Spectroscopic and metal-binding properties of DF3: an artificial protein able to accommodate different metal ions
The design, synthesis, and metal-binding properties of DF3, a new de novo designed di-iron protein model are described (“DF” represents due ferri, Italian for “two iron,” “di-iron”). DF3 is the latest member of the DF family of synthetic proteins. They consist of helix–loop–helix hairpins, designed to dimerize and form an antiparallel four-helix bundle that encompasses a metal-binding site similar to those of non-heme carboxylate-bridged di-iron proteins. Unlike previous DF proteins, DF3 is highly soluble in water (up to 3 mM) and forms stable complexes with several metal ions (Zn, Co, and Mn), with the desired secondary structure and the expected stoichiometry of two ions per protein. UV–vis studies of Co(II) and Fe(III) complexes confirm a metal-binding environment similar to previous di-Co(II)- and di-Fe(III)-DF proteins, including the presence of a µ-oxo-di-Fe(III) unit. Interestingly, UV–vis, EPR, and resonance Raman studies suggest the interaction of a tyro-sine adjacent to the di-Fe(III) center. The design of DF3 was aimed at increasing the accessibility of small molecules to the active site of the four-helix bundle. Indeed, binding of azide to the di-Fe(III) site demonstrates a more accessible metal site compared with previous DFs. In fact, fitting of the binding curve to the Hill equation allows us to quantify a 150% accessibility enhancement, with respect to DF2. All these results represent a significant step towards the development of a functional synthetic DF metalloprotein.
The design, synthesis, and metal-binding properties of DF3, a new de novo designed di-iron protein model are described (“DF” represents due ferri, Italian for “two iron,” “di-iron”). DF3 is the latest member of the DF family of synthetic proteins. They consist of helix–loop–helix hairpins, designed to dimerize and form an antiparallel four-helix bundle that encompasses a metal-binding site similar to those of non-heme carboxylate-bridged di-iron proteins. Unlike previous DF proteins, DF3 is highly soluble in water (up to 3 mM) and forms stable complexes with several metal ions (Zn, Co, and Mn), with the desired secondary structure and the expected stoichiometry of two ions per protein. UV–vis studies of Co(II) and Fe(III) complexes confirm a metal-binding environment similar to previous di-Co(II)- and di-Fe(III)-DF proteins, including the presence of a µ-oxo-di-Fe(III) unit. Interestingly, UV–vis, EPR, and resonance Raman studies suggest the interaction of a tyro-sine adjacent to the di-Fe(III) center. The design of DF3 was aimed at increasing the accessibility of small molecules to the active site of the four-helix bundle. Indeed, binding of azide to the di-Fe(III) site demonstrates a more accessible metal site compared with previous DFs. In fact, fitting of the binding curve to the Hill equation allows us to quantify a 150% accessibility enhancement, with respect to DF2. All these results represent a significant step towards the development of a functional synthetic DF metalloprotein.
Spectroscopic and metal-binding properties of DF3: an artificial protein able to accommodate different metal ions
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Spectroscopic and metal-binding properties of DF3: an artificial protein able to accommodate different metal ions
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Impact Factor: 5.476
View Export to BibTeX Export to EndNote
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Impact Factor: 8.091
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Impact Factor: 5.454
View Export to BibTeX Export to EndNote
Manetto GD, Grasso DM, Milardi D, Pappalardo M, Guzzi R, Sportelli L, Verbeet MP, Canters GW, La Rosa C
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Impact Factor: 3.446
View Export to BibTeX Export to EndNote
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Impact Factor: 2.545
View Export to BibTeX Export to EndNote
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* Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: A molecular analysis of its reduced thermal stability (1213 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2004 May 25; 43(20): 6043-6058.
Impact Factor: 4.008
View Export to BibTeX Export to EndNote
Pedone E, Bartolucci S, Rossi M, Pierfederici FM, Scire A, Cacciamani T, Tanfani F
* Structural and thermal stability analysis of Escherichia coli and Alicyclobacillus acidocaldarius thioredoxin revealed a molten globule-like state in thermal denaturation pathway of the proteins: an infrared spectroscopic study (837 views)
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Impact Factor: 4.101
View Export to BibTeX Export to EndNote
Maglio O, Saldanha JW, Vrtala S, Spitzauer S, Valenta R, Pastore A
* A major IgE epitope-containing grass pollen allergen domain from Phl p 5 folds as a four-helix bundle (668 views)
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Impact Factor: 2.126
View Export to BibTeX Export to EndNote
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* Valine114 Replacements In The Archaeal Elongation Factor 1a Enhanced Its Ability To Interact With Aminoacyl-Trna And Kirromycin (468 views)
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Impact Factor: 4.064
View Export to BibTeX Export to EndNote
Bonomo RP, Bonsignore F, Conte E, Impellizzeri G, Pappalardo G, Purrello R, Rizzarelli E
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J Chem Soc (ISSN: 1364-5447), 1993; 8: 1295-1300.
Impact Factor: 0
View Export to BibTeX Export to EndNote
25 Records (23 excluding Abstracts).
Total impact factor: 119.852 (114.693 excluding Abstracts).
Total 5 year impact factor: 111.408 (106.181 excluding Abstracts).
Total impact factor: 119.852 (114.693 excluding Abstracts).
Total 5 year impact factor: 111.408 (106.181 excluding Abstracts).
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