Sanina, N.A., Syrtsova, L.A., Shkondina, N.I., Rudneva, T.N., Malkova, E.S., Bazanov, T.A., Kotel’nikov, A.I. and Aldoshin, S.M. (2007) Reaction of Sulfur-Nitrosyl Iron Complexes of “g = 2.03” Family with Hemoglobin (Hb): Kinetics of Hb-NO Formation in Aqueous Solutions. Nitric Oxide: Biology and Chemistry, 16, 181-188.
http://dx.doi.org/10.1016/j.niox.2006.10.005

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.