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Antonini, E. and Brunori, M. (1971) Hemoglobin and Myoglobin in the Reactions with Ligands. In: Neuberger, A. and Tatum, E.L., Eds., North-Holland Research Monographs. Frontiers of Biology, Vol. 21, North-Holland Publishing Company, Amsterdam and London, 276.

has been cited by the following article:

• TITLE: Interaction of Hemoglobin with Binuclearcationic Tetranitrosyl Iron Complex with Penicillamine. Cations Binding Sites

  AUTHORS: Lidia Syrtsova, Natalia Sanina, Boris Psikha, Ildar Tukhvatullin, Natal’ja Shkondina, Olesia Pokidova, Alexander Kotelnikov

  KEYWORDS: Biomedicine, Iron-Sulfur Cluster, Ligand Binding, Heme, Nitric Oxide

  JOURNAL NAME: Advances in Biological Chemistry, Vol.5 No.3, April 28, 2015

  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.