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Titolo:
SOLVENT EFFECTS ON THE DISTRIBUTION OF CONFORMATIONAL SUBSTATES IN NATIVE AND AZIDE REACTED CU, ZN SUPEROXIDE-DISMUTASE - AN EPR STUDY
Autore:
POLIZIO F; BIZZARRI AR; CANNISTRARO S; DESIDERI A;
Indirizzi:
UNIV ROMA TOR VERGATA,INFM,DIPARTIMENTO BIOL I-00173 ROME ITALY UNIV ROMA TOR VERGATA,INFM,DIPARTIMENTO BIOL I-00173 ROME ITALY UNIV TUSCIA,DIPARTIMENTO SCI AMBIENTALI I-01100 VITERBO ITALY UNIV PERUGIA,INFM,DIPARTIMENTO FIS I-06100 PERUGIA ITALY
Titolo Testata:
European biophysics journal
fascicolo: 4, volume: 26, anno: 1997,
pagine: 291 - 297
SICI:
0175-7571(1997)26:4<291:SEOTDO>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTRON-PARAMAGNETIC-RES; TEMPERATURE OPTICAL SPECTROSCOPY; STRUCTURAL DYNAMICS; G-STRAIN; NEUTRON-SCATTERING; MYOGLOBIN CRYSTALS; PROTEIN DYNAMICS; COPPER PROTEINS; METAL SITES; SPECTRA;
Keywords:
SUPEROXIDE DISMUTASE; CONFORMATIONAL SUBSTATES; ELECTRONIC PARAMAGNETIC RESONANCE; SOLVENT EFFECT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
50
Recensione:
Indirizzi per estratti:
Citazione:
F. Polizio et al., "SOLVENT EFFECTS ON THE DISTRIBUTION OF CONFORMATIONAL SUBSTATES IN NATIVE AND AZIDE REACTED CU, ZN SUPEROXIDE-DISMUTASE - AN EPR STUDY", European biophysics journal, 26(4), 1997, pp. 291-297

Abstract

Native and azide reacted Cu, Zn superoxide dismutase in aqueous and mixed water-glycerol solution have been investigated by EPR spectroscopy at low temperature. An accurate computer simulation, based on a wellestablished theoretical model which has been reformulated for rhombicsymmetry, has shown that the EPR spectrum of the copper ion in the native protein shows a significant g and A strain in the parallel region. The strain arises from a distribution of the ligand field strengths onto the metal ion and this could be traced back to the existence of amultiplicity of conformational states in the protein molecule. The strain is reduced in the presence of azide which is known to bind directly to the copper atom and to give rise to a more relaxed configurationcorresponding to a square pyramidal geometry in which the apical ligand occupies an elongated position. In both samples, addition of glycerol further reduces the strain, indicating that the solvent is directlycoupled to the protein matrix, thereby modulating the structural heterogeneity displayed by the protein molecule.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 22:03:06