期刊
JOURNAL OF FLUORESCENCE
卷 21, 期 3, 页码 1311-1318出版社
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s10895-010-0816-9
关键词
Quercetin; Lipoxygenase; Flavonoids; Fluorescence; Antioxidants
资金
- Junta de Extremadura (FEDER) [PRI07A041, GRU09042]
- Junta de Extremadura
The interaction between quercetin and lipoxygenase was investigated by fluorescence spectroscopy. The analysis of the emission quenching at different temperatures revealed that the quenching mechanism correspond to a static process and, as consequence, a complex quercetin-lipoxygenase is formed. The thermodynamic parameters Delta G, Delta H and Delta S were calculated to be-32.57 kJmol(-1),-3.21 kJmol(-1) and 87.14 Jmol(-1)K(-1) respectively, which suggest that hydrophobic forces plays a major role in the stabilization of the complex quercetin-lipoxygenase. The distance, r, between donor (lipoxygenase) and acceptor (quercetin) was calculated to be 3.84 nm based on Forster's non-radiative energy transfer theory. The results obtained from the evaluation of three dimensional florescence spectra suggest a conformational modification of the protein in the region of the coupling with quercetin.
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