Impact Factor 2021 = 1.200 has been issued by ISI Web of Knowledge (JCR 2021).

SCImago Journal & Country Rank

ISSN 1998-9539

Thermodynamic Aspects of Binding Proteins with Porphyrins. Spectral and Thermochemical Approaches

Natalya Sh. Lebedeva,a Yury A. Gubarev,a Alexey V. Lyubimtsev,b Elena S. Yurina,a  and Oskar I. Koifmanb

aG.A. Krestov Institute of Solution Chemistry of Russian Academy of Sciences, 153045 Ivanovo, Russia

bResearch Institute of Macroheterocycles, Ivanovo State University of Chemistry and Technology, 153000 Ivanovo, Russia


DOI: 10.6060/mhc160530g

Macroheterocycles 2017 10(1) 37-42


The results of spectral and thermochemical studies of the interaction of bovine serum albumin with anionic and cationic porphyrins are presented in this paper. The limits of different methods for the determination of binding constants and thermodynamic parameters were shown. On the basis of spectral studies the binding constants of albumin with the porphyrins were evaluated. The fluorescence quenching constants of the protein at the porphyrins titration were estimated and it was found that in the albumin-porphyrin systems the static and dynamic quenching mechanisms are combined. The thermodynamic parameters were determined using of Van’t Hoff equation from spectral data and the method of isothermal titration calorimetry. It was established that the stability constant of anionic complex is higher than that for complex of cationic porphyrin with albumin.


mhc160530g.pdf788.53 KB