Copper(II) complexes of prion protein PEG11-tetraoctarepeat fragment: spectroscopic and voltammetric studies (486 views)
Dalton T (ISSN: 1477-9226, 1477-7922, 1477-9234), 2009 Apr 14; (14): 2637-2646.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 2.908, 5-year impact factor: 3.138
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-66349087433&partnerID=40&md5=51121d3d019206683603f12671ce2646
Keywords: Carbonyl Oxygen Atoms, Cooperativity, Coordination Sites, Copper Atoms, Copper Complexes, Copper Sites, Electron Transfer Process, Epr Parameters, Frozen Solutions, Intermediate Complex, Neutral Ph, Nitrogen Atom, Prion Protein, Pyramidal Geometries, Spectroscopic Data, Voltammetric Measurements, Voltammetric Studies, Bioelectric Phenomena, Chromophores, Coordination Reactions, Electron Resonance, Electron Spin Resonance Spectroscopy, Paramagnetic Resonance, Polyethylene Glycols, Quantum Theory, Copper Compounds, Ligand, Nitric Oxide, Organometallic Compound, Peptide, Article, Chemistry, Electrochemistry, Ultraviolet Spectrophotometry, Electrodes, Copper Chemistry, Nitric Oxide Chemistry, Organometallic Compounds Chemistry, Peptides Chemistry, Prions Chemistry,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Universita di Catania, Viale A. Doria 6, 95125, Catania, Italy. rbonomo@unict. it
Istituto di Biostrutture e Bioimmagini, CNR, Unit Organizzativa di Supporto di Catania, Viale A. Doria 6, 95125, Catania, Italy
References:
Not available.
Dalton T (ISSN: 1477-9226, 1477-7922, 1477-9234), 2009 Apr 14; (14): 2637-2646.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 2.908, 5-year impact factor: 3.138
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-66349087433&partnerID=40&md5=51121d3d019206683603f12671ce2646
Keywords: Carbonyl Oxygen Atoms, Cooperativity, Coordination Sites, Copper Atoms, Copper Complexes, Copper Sites, Electron Transfer Process, Epr Parameters, Frozen Solutions, Intermediate Complex, Neutral Ph, Nitrogen Atom, Prion Protein, Pyramidal Geometries, Spectroscopic Data, Voltammetric Measurements, Voltammetric Studies, Bioelectric Phenomena, Chromophores, Coordination Reactions, Electron Resonance, Electron Spin Resonance Spectroscopy, Paramagnetic Resonance, Polyethylene Glycols, Quantum Theory, Copper Compounds, Ligand, Nitric Oxide, Organometallic Compound, Peptide, Article, Chemistry, Electrochemistry, Ultraviolet Spectrophotometry, Electrodes, Copper Chemistry, Nitric Oxide Chemistry, Organometallic Compounds Chemistry, Peptides Chemistry, Prions Chemistry,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Universita di Catania, Viale A. Doria 6, 95125, Catania, Italy. rbonomo@unict. it
Istituto di Biostrutture e Bioimmagini, CNR, Unit Organizzativa di Supporto di Catania, Viale A. Doria 6, 95125, Catania, Italy
References:
Not available.
Copper(II) complexes of prion protein PEG11-tetraoctarepeat fragment: spectroscopic and voltammetric studies
Spectroscopic (UV-Vis and EPR) and voltammetric studies have been carried out on the copper (ii) complexes with the Ac-PEG11- (PHGGGWGQ) 4-NH2 (L) polypeptide. In the ratios Cu: L 3: 1 and 4: 1, the two [Cu3 (L) H-6] and [Cu4 (L) H-8] complex species have been characterized at neutral pH values. All the copper atoms occupy similar coordination sites formed by imidazole, peptidic nitrogen atoms and carbonyl oxygen atoms in a square base pyramidal geometry. Voltammetric measurements on these systems point out the cooperativity in the electron transfer processes among the copper (ii) sites during their reduction. NO interaction with these polynuclear copper species is characterized by the reduction of the copper sites through the formation of two different intermediate complex species. When an excess of the Ac-PEG11- (PHGGGWGQ) 4-NH2 ligand is considered, frozen solution EPR parameters and UV-Vis spectroscopic data identify the [Cu (Nim) 4] 2+ chromophore, which does not interact with NO. 2009 The Royal Society of Chemistry
Spectroscopic (UV-Vis and EPR) and voltammetric studies have been carried out on the copper (ii) complexes with the Ac-PEG11- (PHGGGWGQ) 4-NH2 (L) polypeptide. In the ratios Cu: L 3: 1 and 4: 1, the two [Cu3 (L) H-6] and [Cu4 (L) H-8] complex species have been characterized at neutral pH values. All the copper atoms occupy similar coordination sites formed by imidazole, peptidic nitrogen atoms and carbonyl oxygen atoms in a square base pyramidal geometry. Voltammetric measurements on these systems point out the cooperativity in the electron transfer processes among the copper (ii) sites during their reduction. NO interaction with these polynuclear copper species is characterized by the reduction of the copper sites through the formation of two different intermediate complex species. When an excess of the Ac-PEG11- (PHGGGWGQ) 4-NH2 ligand is considered, frozen solution EPR parameters and UV-Vis spectroscopic data identify the [Cu (Nim) 4] 2+ chromophore, which does not interact with NO. 2009 The Royal Society of Chemistry
Copper(II) complexes of prion protein PEG11-tetraoctarepeat fragment: spectroscopic and voltammetric studies
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Copper(II) complexes of prion protein PEG11-tetraoctarepeat fragment: spectroscopic and voltammetric studies
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Impact Factor: 3.838
View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2010 Sep 14; 39(30): 7046-7053.
Impact Factor: 3.647
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 (1328 views)
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Impact Factor: 5.476
View Export to BibTeX Export to EndNote
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Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2010; 39(30): 7046-7053.
Impact Factor: 3.647
View Export to BibTeX Export to EndNote
Bonomo RP, Pappalardo G, Rizzarelli E, Santoro AM, Tabbì G, Vagliasindi LI
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Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2007 Apr 14; (14): 1400-1408.
Impact Factor: 3.212
View Export to BibTeX Export to EndNote
Mazzarella L, Vergara A, Vitagliano L, Merlino A, Bonomi G, Scala S, Verde C, Di Prisco G
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Impact Factor: 3.73
View Export to BibTeX Export to EndNote
Mazzarella L, Bonomi G, Lubrano MC, Merlino A, Riccio A, Vergara A, Vitagliano L, Verde C, Di Prisco G
* Minimal structural requirements for root effect: Crystal structure of the cathodic hemoglobin isolated from the Antarctic fish Trematomus newnesi (624 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2006 Feb 1; 62(2): 316-321.
Impact Factor: 3.73
View Export to BibTeX Export to EndNote
Campagna T, Grasso G, Rizzarelli E, Vecchio G
L- and D-cysteine derivatives of β-cyclodextrin: Different molecular recognition properties of their copper(II) complexes for amino acids (426 views)
Inorg Chim Acta (ISSN: 0020-1693), 1998; 275-276: 395-400.
Impact Factor: 1.454
View Export to BibTeX Export to EndNote
Marletta F, Rizzarelli E, Mangiameli A, Brogna A, Sammartano S, Monaco S, Blasi A
Effects of graded doses of copper complexes of L-aminoacids on gastric acid secretion in rats (1374 views)
Boll Soc Ital Biol Sper (ISSN: 0037-8771), 1979 Apr 30; 55(8): 769-775.
Impact Factor: 0
View Export to BibTeX Export to EndNote
18 Records (18 excluding Abstracts).
Total impact factor: 67.046 (67.046 excluding Abstracts).
Total 5 year impact factor: 66.408 (66.408 excluding Abstracts).
Total impact factor: 67.046 (67.046 excluding Abstracts).
Total 5 year impact factor: 66.408 (66.408 excluding Abstracts).
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