Analysis of the binding interaction in uric acid - Human hemoglobin system by spectroscopic techniques.
The binding interaction between human hemoglobin and uric acid has been studied for the first time, by UV-vis absorption and steady-state, synchronous and three-dimensional fluorescence techniques. Characteristic effects observed for human hemoglobin intrinsic fluorescence during interaction with uric acid at neutral pH point at the formation of stacking non-covalent and non-fluorescent complexes. All the calculated parameters, the binding, fluorescence quenching and bimolecular quenching rate constants, as well as Förster resonance energy transfer parameters confirm the existence of static quenching. The results of synchronous fluorescence measurements indicate that the fluorescence quenching of human hemoglobin originates both from Trp and Tyr residues and that the addition of uric acid could significantly hinder the physiological functions of human hemoglobin.
Department of Inorganic Chemistry, Maria Curie-Sklodowska University, M. C. Sklodowska Sq. 2, 20-031 Lublin, Poland. Electronic address: makarska@hektor.umcs.lublin.pl.
Magdalena
M
Makarska-Bialokoz
D001665:Binding Sites; D031541:Fluorescence Resonance Energy Transfer; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D011485:Protein Binding; D013056:Spectrophotometry, Ultraviolet; D014527:Uric Acid / Q000737:chemistry / Q000378:metabolism*
D006454:Hemoglobins; D014527:Uric Acid
FRET; Fluorescence quenching; Human hemoglobin; Uric acid