title: Interaction of m-nitrophenylfluorone-Mo(VI) complex as a probe with human serum albumin: a fluorescence quenching study.
abstract: In this paper, the binding characteristics of human serum albumin (HSA) and m-nitrophenylfluorone (m-NPF)-molybdenum (Mo(VI)) complex have been studied by fluorophotometry. The binding constants are measured at different temperature. Based on the theory of Forster energy transfer, the binding distance and the energy transfer efficiency between m-nitrophenylfluorone-Mo(VI) complex and protein are obtained. According to the thermodynamic parameters, the main sort of binding force can be judged. The results indicate that HSA and m-NPF-Mo(VI) complex have strong interactions. The mechanism of quenching belongs to static quenching and the main sort of binding force is electrostatic gravitation.
authors.affiliation: School of Chemistry & Chemical Engineering, Jinan University, Jinan 250022, PR China. sdjndxwq@263.net
authors.forename: Qin
authors.initials: Q
authors.lastname: Wei
authors.forename: Dan
authors.initials: D
authors.lastname: Wu
authors.forename: Bin
authors.initials: B
authors.lastname: Du
authors.forename: Yan
authors.initials: Y
authors.lastname: Li
authors.forename: Caihong
authors.initials: C
authors.lastname: Duan
mesh_terms: D004735:Energy Transfer; D005452:Fluoresceins / Q000737:chemistry*; D005456:Fluorescent Dyes / Q000494:pharmacology*; D006801:Humans; D006860:Hydrogen Bonding; D008956:Models, Chemical; D008982:Molybdenum / Q000737:chemistry*; D009942:Organometallic Compounds / Q000737:chemistry*; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*; D049993:Sodium Chloride Symporter Inhibitors / Q000737:chemistry; D013050:Spectrometry, Fluorescence / Q000379:methods*; D055672:Static Electricity; D013696:Temperature; D013816:Thermodynamics
chemical_list: D005452:Fluoresceins; D005456:Fluorescent Dyes; D009942:Organometallic Compounds; D012709:Serum Albumin; D049993:Sodium Chloride Symporter Inhibitors; C010159:fluorone Black; D008982:Molybdenum