Výsledky vyhledávání - "M. E. Stroppolo"

Dynamics-Function Correlation in Cu, Zn Superoxide Dismutase: A Spectroscopic and Molecular Dynamics Simulation Study

Autor: Mauro Ferrario, M. E. Stroppolo, Alessandro Desideri, Patrizia Cioni, Alessandro Sergi, Mattia Falconi, Giovanni B. Strambini

Publikováno v: Scopus-Elsevier
Mauro Ferrario

A single mutation (Val29→Gly) at the subunit interface of a Cu, Zn superoxide dismutase dimer leads to a twofold increase in the second order catalytic rate, when compared to the native enzyme, without causing any modification of the structure or t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f07b2e656813d90ec98813e14b6fc81f
https://doi.org/10.1016/s0006-3495(01)76227-3

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Single mutations at the subunit interface modulate copper reactivity in Photobacterium leiognathi Cu,Zn superoxide dismutase

Autor: M. E. Stroppolo, Mario Milani, Alessandro Desideri, Camillo Rosano, Alessandra Pesce, Martino Bolognesi, Domenico Bordo, Melania D'Orazio, Peter O'Neill, Andrea Battistoni

Publikováno v: Journal of Molecular Biology. 308:555-563

The functional properties and X-ray structures of five mutant forms of Photobacterium leiognathi Cu,Zn superoxide dismutase carrying single mutations at residues located at the dimer association interface have been investigated. When compared to the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80fbda25503869f893608eed5a51e9e8
https://doi.org/10.1006/jmbi.2001.4606

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Functional and crystallographic characterization of Salmonella typhimurium Cu,Zn superoxide dismutase coded by the sodCI virulence gene 1 1Edited by R. Huber

Autor: Alessandra Pesce, Martino Bolognesi, Francesca Polizio, M. E. Stroppolo, Marco Nardini, J S Kroll, Paul R. Langford, Peter O'Neill, Marco Sette, Andrea Battistoni, Alessandro Desideri

Publikováno v: Journal of Molecular Biology. 302:465-478

The functional and three-dimensional structural features of Cu,Zn superoxide dismutase coded by the Salmonella typhimurium sodCI gene, have been characterized. Measurements of the catalytic rate indicate that this enzyme is the most efficient superox

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::18f2aee509c2cd24c92e82d173b59d02
https://doi.org/10.1006/jmbi.2000.4074

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Low-Temperature Optical Spectroscopy of Native and Azide-Reacted Bovine Cu,Zn Superoxide Dismutase. A Structural Dynamics Study

Autor: Antonio Cupane, Maurizio Leone, Fabio Polticelli, Alessandro Desideri, Militello, M. E. Stroppolo

Publikováno v: Biochemistry. 33:15103-15109

The optical absorption spectra of native and N(3-)-reacted Cu,Zn superoxide dismutase (SOD) has been studied in the temperature range 300-10 K. The broad d-d bands observed in the room temperature spectrum, centered at 14,700 cm-1 (native enzyme) and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72aef4b08a637ea3ef6744752bb6adf9
https://doi.org/10.1021/bi00254a020

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A comparative study on the anion binding properties of Bos taurus and Prionace glauca Cu,Zn superoxide dismutases native and chemically modified at lysines

Autor: S. Costanzo, Francesca Polizio, Raffaele Petruzzelli, Amalia Lania, F. Polticelli, M. E. Stroppolo, Alessandro Desideri, Antonio Galtieri

Publikováno v: Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology. 109:141-145

The interaction between the competitive inhibitor azide and ox and shark Cu,Zn Superoxide dismutases (SODs), in the native state and chemically modified at lysines, has been investigated by optical and EPR spectroscopy. The affinity constants for the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::77ca23fc847552da680ef656fe03e90d
https://doi.org/10.1016/0742-8413(94)00052-c

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Experimental and simulative dissociation of dimeric Cu, Zn superoxide dismutase doubly mutated at the intersubunit surface

Autor: Giovanni B. Strambini, Luca Maragliano, Alessandro Desideri, Mattia Falconi, Patrizia Cioni, Amalia Lania, M. E. Stroppolo, Alessandro Sergi, Mauro Ferrario, Silvia Castelli

Publikováno v: Biophysical journal
88 (2005): 2875–2882.
info:cnr-pdr/source/autori:Maragliano L, Falconi M, Sergi A, Cioni P, Castelli S, Lania A, Stroppolo ME, Strambini G, Ferrario M, Desideri A./titolo:Experimental and simulative dissociation of dimeric Cu,Zn superoxide dismutase doubly mutated at the intersubunit surface./doi:/rivista:Biophysical journal (Print)/anno:2005/pagina_da:2875/pagina_a:2882/intervallo_pagine:2875–2882/volume:88

The equilibrium properties of dimeric Photobacterium leiognathi Cu,Zn superoxide dismutase mutant bearing two negative charges in the amino acid clusters at the association interface has been studied, experimentally and computationally, and compared

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a3e5ee3579b8d7b4449d4f1dd828629
https://hdl.handle.net/11380/306820

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On the coordination and oxidation states of the active-site copper ion in prokaryotic Cu,Zn superoxide dismutases

Autor: Camillo Rosano, S. Nuzzo, Andrea Battistoni, M. E. Stroppolo, Alessandro Desideri, Alessandra Pesce, Settimio Mobilio, Martino Bolognesi

The active-site copper ion of the prokaryotic Cu,Zn superoxide dismutase from P. leiognathi is found to undergo reversible reduction upon irradiation of the protein solution with a high-intensity X-ray beam from a third-generation synchrotron source.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a45563a10b51e7db196c7742433f73f
http://hdl.handle.net/2108/55143

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Spectroscopic characterization of recombinant Cu,Zn superoxide dismutase from Photobacterium leiognathi expressed in Escherichia coli: evidence for a novel catalytic copper binding site

Autor: G. Cuzzocrea, B. Lo Curto, M. E. Stroppolo, D. Foti, Mariano Venanzi, Francesca Polizio, Alessandro Desideri

Publikováno v: Biochemistry. 36(23)

Cu,Zn superoxide dismutase from Photobacterium leiognathi has been cloned and expressed in Escherichia coli. The circular dichroism spectrum in the UV region of the recombinant protein indicates an higher content of random coil structure with respect

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ebfedb2d8e49bbf36b8ad1197fc08a9
https://pubmed.ncbi.nlm.nih.gov/9188710

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Low-temperature optical spectroscopy of cobalt in Cu,Co superoxide dismutase: a structural dynamics study of the solvent-unaccessible metal site

Autor: Militello, Fabio Polticelli, Alessandro Desideri, Maurizio Leone, Antonio Cupane, M. E. Stroppolo

Publikováno v: Biochemistry. 34(50)

The temperature dependence (300 to 10 K) of the electronic absorption spectra of the cobalt chromophore in bovine superoxide dismutase (SOD) having the native Zn(II) ion selectivity replaced by Co(II) has been investigated in four different derivativ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08e2d3aea37d5038e18436da066e7a2f
https://pubmed.ncbi.nlm.nih.gov/8845356

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