Quenching of the intrinsic fluorescence of bovine serum albumin by phenylfluorone–Mo(VI) complex as a probe

Abstract

In this paper, the binding characteristics of bovine serum albumin (BSA) and phenylfluorone (PF)–molybdenum (Mo(VI)) complex have been studied by fluorophotometry. The binding constants are calculated at different temperatures. The binding distance and the energy transfer efficiency between PF–Mo(VI) complex and protein are obtained on the basis of the theory of Forster energy transfer. Δ H and Δ S are calculated to be −7.11 kJ mol −1 and 70.30 J mol −1 K −1, which indicate that electrostatic force plays major role in the interaction of PF–Mo(VI) complex and BSA. The experimental results show that BSA and PF–Mo(VI) complex have strong interactions and the mechanism of quenching belongs to static quenching.