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

Lebedevа, N. Sh.; Gubarev, Yury A.; Lyubimtsev, Alexey; Yurina, Elena S.; Койфман, О. И.

doi:10.6060/mhc160530g

Cited by 3 publications

References 25 publications

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Characterization of the complex between native and reduced bovine serum albumin with aquacobalamin and evidence of dual tetrapyrrole binding

et al. 2018

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Serum albumin binds to a variety of endogenous ligands and drugs. Human serum albumin (HSA) binds to heme via hydrophobic interactions and axial coordination of the iron center by protein residue Tyr161. Human serum albumin binds to another tetrapyrrole, cobalamin (Cbl), but the structural and functional properties of this complex are poorly understood. Herein, we investigate the reaction between aquacobalamin (HOCbl) and bovine serum albumin (BSA, the bovine counterpart of HSA) using Ultraviolet-Visible and fluorescent spectroscopy, and electron paramagnetic resonance. The reaction between HOCbl and BSA led to the formation of a BSA-Cbl(III) complex consistent with N-axial ligation (amino). Prior to the formation of this complex, the reactants participate in an additional binding event that has been examined by fluorescence spectroscopy. Binding of BSA to Cbl(III) reduced complex formation between the bound cobalamin and free cyanide to form cyanocobalamin (CNCbl), suggesting that the β-axial position of the cobalamin may be occupied by an amino acid residue from the protein. Reaction of BSA containing reduced disulfide bonds with HOCbl produces cob(II)alamin and disulfide with intermediate formation of thiolate Cbl(III)-BSA complex and its decomposition. Finally, in vitro studies showed that cobalamin binds to BSA only in the presence of an excess of protein, which is in contrast to heme binding to BSA that involves a 1:1 stoichiometry. In vitro formation of BSA-Cbl(III) complex does not preclude subsequent heme binding, which occurs without displacement of HOCbl bound to BSA. These data suggest that the two tetrapyrroles interact with BSA in different binding pockets.

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Characterization of the complex between native and reduced bovine serum albumin with aquacobalamin and evidence of dual tetrapyrrole binding

et al. 2018

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Exploring the structure of a ruthenium acetate cluster for biological purposes

Silva

Ramos

Rohrabaugh

et al. 2020

Inorganic Chemistry Communications

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Synthesis of anionic and cationic corroles and study of their complexing ability and photodynamic activity towards DNA and albumin

Yurina

Lebedevа

Киселев

et al. 2023

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In this work, new free base corroles (sulfophenylcorrole (mixture of tri(4-sulfophenyl)corrole and tetrasulfotriphenylcorrole) and tri(N-methylpyridin-4-yl)corrole triiodide) were synthesized and associative equilibria in aqueous and organic media were studied. Their binding ability to BSA and DNA was studied by various physicochemical methods. It has been established that complexes with DNA are formed only by cationic corrole, which binds to DNA by the intercalation method. Both cationic and anionic corroles bind to bovine serum albumin. It was found that the synthesized corroles are weakly fluorescent fluorophores and practically do not generate singlet oxygen; however, they are capable of generating superoxide anion radicals; can participate in type I photooxidation. The ability to initiate type I photoprocesses was established on the basis of the processes of photooxidation of nitroblue tetrazolium and BSA. The possibility of potentiating the process of protein photooxidation by potassium iodide has been established. Radical and radical ion reactions underlying the potentiation of BSA oxidation upon photoirradiation with PS were studied. It was found that the addition of KI significantly accelerates the photooxidation of BSA. It has been proven that the stage of formation of triiodide ions, which trigger a cascade of radical ion reactions, plays an important role in the potentiation processes.

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

Cited by 3 publications

References 25 publications

Characterization of the complex between native and reduced bovine serum albumin with aquacobalamin and evidence of dual tetrapyrrole binding

Characterization of the complex between native and reduced bovine serum albumin with aquacobalamin and evidence of dual tetrapyrrole binding

Exploring the structure of a ruthenium acetate cluster for biological purposes

Synthesis of anionic and cationic corroles and study of their complexing ability and photodynamic activity towards DNA and albumin

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