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Titolo:
AN EPR INVESTIGATION ON THE STRUCTURAL HETEROGENEITY IN COPPER AZURINAND PLASTOCYANIN
Autore:
GUZZI R; BIZZARRI AR; SPORTELLI L; CANNISTRARO S;
Indirizzi:
UNIV TUSCIA,DIPARTIMENTO SCI AMBIENTALI I-01100 VITERBO ITALY UNIV TUSCIA,DIPARTIMENTO SCI AMBIENTALI I-01100 VITERBO ITALY UNIV CALABRIA,DIPARTIMENTO FIS,UNITA INFM I-87030 ARCAVACATA CS ITALY UNIV PERUGIA,DIPARTIMENTO FIS,UNITA INFM I-06100 PERUGIA ITALY
Titolo Testata:
Biophysical chemistry
fascicolo: 2-3, volume: 63, anno: 1997,
pagine: 211 - 219
SICI:
0301-4622(1997)63:2-3<211:AEIOTS>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTRON-PARAMAGNETIC-RES; G-STRAIN; PSEUDOMONAS-AERUGINOSA; COMPUTER-SIMULATION; MYOGLOBIN CRYSTALS; FREQUENCY-SWEPT; FIELD-SWEPT; PROTEIN; SPECTRA; GLASSES;
Keywords:
ELECTRON PARAMAGNETIC RESONANCE; AZURIN; PLASTOCYANIN; FREEZING RATE; GLYCEROL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
R. Guzzi et al., "AN EPR INVESTIGATION ON THE STRUCTURAL HETEROGENEITY IN COPPER AZURINAND PLASTOCYANIN", Biophysical chemistry, 63(2-3), 1997, pp. 211-219

Abstract

The effects of cooling rate and of solvent properties on the active site heterogeneity of two copper proteins, azurin and plastocyanin, have been investigated at low temperature by electron paramagnetic resonance spectroscopy. The spectra of theses proteins have been analyzed, by an accurate computer simulation, in terms of a distribution of some relevant spin-Hamiltonian parameters. The results show that the structural heterogeneity of both proteins, quantified by the width of the distribution in the g and A tensors, is affected by both the freezing procedure and the solvent composition. In particular, the g distributionwidth is found to be reduced in the slow cooling regime; such a reduction appearing more significant when glycerol is added to the protein solutions. Despite of the similarity in the copper ion microenvironments of the two proteins, the effects are more pronounced in azurin. Theresults are discussed also in connection with the role played by the solvent and the rate of freezing in featuring the conformational substate landscape. (C) 1997 Elsevier Science B.V.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 00:56:49