1. Interaction of Hemoglobin with Binuclearcationic Tetranitrosyl Iron Complex with Penicillamine. Cations Binding Sites
- Author
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Ildar Tukhvatullin, B. L. Psikha, L. A. Syrtsova, N. I. Shkondina, Alexander I. Kotelnikov, Olesia Pokidova, and Natalia A. Sanina
- Subjects
Kinetics ,Penicillamine ,Inorganic chemistry ,Iron–sulfur cluster ,Coupling reaction ,chemistry.chemical_compound ,Crystallography ,chemistry ,medicine ,Pharmacology (medical) ,Hemoglobin ,Binding site ,Heme ,Equilibrium constant ,medicine.drug - Abstract
In this paper, the kinetics of the interaction of the nitrosyl iron complex with the ligands penicillamine [Fe2(SC5H11NО2)2(NO)4]SO4·5H2O (I) with deoxyhemoglobin (Hb) was studied. The kinetic modeling method defined the number of binding (I) molecules and equilibrium constant of the coupling reaction of (Biomedicine, Iron-Sulfur Cluster, Ligand Binding, Heme, Nitric Oxide ) with Hb (Ks). At equimolar concentrations of (I) and Hb (2 × 10−5 M), the Hb molecule binds only one (I) with Ks equal to 4.3 × 107 M−1. When increasing the (Biomedicine, Iron-Sulfur Cluster, Ligand Binding, Heme, Nitric Oxide ) concentration, the number of binding sites of Hb increases and Ks decreases. These results are analyzed in accordance with the data on the existence of cations binding sites in Hb.
- Published
- 2015
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