title: 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. 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.
authors.affiliation: Key Laboratory of Colloid and Interface Chemistry, Shandong University, Jinan 250100, PR China.
authors.forename: Dan
authors.initials: D
authors.lastname: Wu
authors.forename: Qin
authors.initials: Q
authors.lastname: Wei
authors.forename: Yan
authors.initials: Y
authors.lastname: Li
authors.forename: Bin
authors.initials: B
authors.lastname: Du
authors.forename: Guiying
authors.initials: G
authors.lastname: Xu
mesh_terms: D000818:Animals; D001671:Biochemistry / Q000379:methods*; D002417:Cattle; D004735:Energy Transfer; D005452:Fluoresceins / Q000737:chemistry*; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D005456:Fluorescent Dyes / Q000737:chemistry*; D008956:Models, Chemical; D015233:Models, Statistical; D008982:Molybdenum / Q000737:chemistry*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D055672:Static Electricity; D013696:Temperature; D013816:Thermodynamics
chemical_list: D005452:Fluoresceins; D005456:Fluorescent Dyes; D012710:Serum Albumin, Bovine; C010159:fluorone Black; D008982:Molybdenum