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Titolo:
On the involvement of electron transfer reactions in the fluorescence decay kinetics heterogeneity of proteins
Autore:
Ababou, A; Bombarda, E;
Indirizzi:
Dept Chem, Chandlee Lab 405, University Pk, PA 16802 USA Dept Chem University Pk PA USA 16802 Lab 405, University Pk, PA 16802 USA Univ Strasbourg 1, UMR 7034 CNRS, Illkirch Graffenstaden, France Univ Strasbourg 1 Illkirch Graffenstaden France h Graffenstaden, France
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 10, volume: 10, anno: 2001,
pagine: 2102 - 2113
SICI:
0961-8368(200110)10:10<2102:OTIOET>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
TIME-RESOLVED FLUORESCENCE; PICOSECOND LASER PHOTOLYSIS; QUENCHES INDOLE FLUORESCENCE; STATE PROTON-TRANSFER; EGG-WHITE LYSOZYME; TRYPTOPHAN FLUORESCENCE; SINGLE TRYPTOPHAN; MOLECULAR-DYNAMICS; CHARGE SEPARATION; REDOX POTENTIALS;
Keywords:
tryptophan; photophysics; time-resolved fluorescence; electron transfer;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
91
Recensione:
Indirizzi per estratti:
Indirizzo: Ababou, A Dept Chem, Chandlee Lab 405, University Pk, PA 16802 USA Dept Chem University Pk PA USA 16802 niversity Pk, PA 16802 USA
Citazione:
A. Ababou e E. Bombarda, "On the involvement of electron transfer reactions in the fluorescence decay kinetics heterogeneity of proteins", PROTEIN SCI, 10(10), 2001, pp. 2102-2113

Abstract

Time-resolved fluorescence study of single tryptophan-containing proteins,nuclease, ribonuclease T1, protein G, glucagon, and mastoparan, has been carried out. Three different methods were used for the analysis of fluorescence decays: the iterative reconvolution method, as reviewed and developed in our laboratory, the maximum entropy method, and the recent method that wecalled "energy transfer" method. All the proteins show heterogeneous fluorescence kinetics (multiexponential decay). The origin of this heterogeneityis interpreted in terms of current theories of electron transfer process, which treat the electron transfer process as a radiationless transition. The theoretical electron transfer rate was calculated assuming the peptide bond carbonyl as the acceptor site. The good agreement between experimental and theoretical electron-transfer rates leads us to suggest that the electron-transfer process is the principal quenching mechanism of Trp fluorescencein proteins, resulting in heterogeneous fluorescence kinetics. Furthermore, the origin of apparent homogeneous fluorescence kinetics (monoexponentialdecay) in some proteins also can be explained on the basis of electron-transfer mechanism.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 23:57:57