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

Int J Biol Macromol. 2005 Oct 30;37(1-2):69-72. doi: 10.1016/j.ijbiomac.2005.08.007. Epub 2005 Oct 3.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biochemistry / methods*
  • Cattle
  • Energy Transfer
  • Fluoresceins / chemistry*
  • Fluorescence Resonance Energy Transfer / methods*
  • Fluorescent Dyes / chemistry*
  • Models, Chemical
  • Models, Statistical
  • Molybdenum / chemistry*
  • Protein Binding
  • Serum Albumin, Bovine / chemistry*
  • Spectrometry, Fluorescence
  • Static Electricity
  • Temperature
  • Thermodynamics

Substances

  • Fluoresceins
  • Fluorescent Dyes
  • Serum Albumin, Bovine
  • fluorone Black
  • Molybdenum