Abstract
The interaction between bovine hemoglobin (BHb) and phosphomolybdate acid (PMo 12) was investigated by UV/vis absorption, IR, circular dichroism (CD), fluorescence, resonance light scattering spectra, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. PMo 12 effectively quenched the intrinsic fluorescence of BHb via static quenching. The process of binding PMo 12 on BHb was a spontaneous molecular interaction procedure. The thermodynamic parameters, Δ H° and Δ S° were estimated to be 28.69 K J mol −1, 158.20 J mol −1 K −1 according to the van’ Hoff equation. This indicates that hydrophobic interaction played a major role in stabilizing the PMo 12–BHb complex. The effect of PMo 12 on the conformation of BHb was analyzed using synchronous fluorescence spectroscopy, IR and CD spectra.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
