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• W2046871302 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. DeltaH and DeltaS 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." @default.
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• W2046871302 date "2005-10-01" @default.
• W2046871302 modified "2023-09-27" @default.
• W2046871302 title "Quenching of the intrinsic fluorescence of bovine serum albumin by phenylfluorone–Mo(VI) complex as a probe" @default.
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• W2046871302 doi "https://doi.org/10.1016/j.ijbiomac.2005.08.007" @default.
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