Time-resolved fluorescence study during denaturation and renaturation of curcumin-myoglobin complex |
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Authors: | Patra Digambara Barakat Christelle |
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Affiliation: | Department of Chemistry, American University of Beirut, Beirut, Lebanon. dp03@aub.edu.lb |
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Abstract: | Curcumin influences the transition point, the concentration of denaturant required to effect 50% of the total change, of myoglobin denaturation. Curcumin enhances absorbance of myoglobin at 280 nm with a binding constant K=3.0×10(4) M(-1) whereas fluorescence of curcumin is quenched by myoglobin with a Stern-Volmer association constant of 2.5×10(5) M(-1). Unfolding process of myoglobin-curcumin induces a recovery in fluorescence lifetime loss. The gain in time-resolved fluorescence lifetime during unfolding has been again lost during refolding of curcumin-myoglobin complex by dilution process suggesting partial reversibility of unfolding process for both myoglobin and curcumin-myoglobin complex. |
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