ABC  Vol.5 No.3 , April 2015
Interaction of Hemoglobin with Binuclearcationic Tetranitrosyl Iron Complex with Penicillamine. Cations Binding Sites
ABSTRACT
In this paper, the kinetics of the interaction of the nitrosyl iron complex with the ligands penicillamine [Fe2(SC5H112)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.

Cite this paper
Syrtsova, L. , Sanina, N. , Psikha, B. , Tukhvatullin, I. , Shkondina, N. , Pokidova, O. and Kotelnikov, A. (2015) Interaction of Hemoglobin with Binuclearcationic Tetranitrosyl Iron Complex with Penicillamine. Cations Binding Sites. Advances in Biological Chemistry, 5, 169-178. doi: 10.4236/abc.2015.53013.
References
[1]   Lancaster, J.R. (2010) Metal-Catalyzed Nitric Oxide Nitrozo Interconversions and Biological Signaling. Nitric Oxide: Biology and Chemistry, 22, 13.

[2]   Lewandowska, H., Kalinowska, M., Brzoska, K., Wojciuk, K., Wojciuk, G. and Kruszewski, M. (2011) Nitrosyl Iron Complexes—Synthesis, Structure and Biology. Dalton Transactions, 40, 8273-8289.
http://dx.doi.org/10.1039/c0dt01244k

[3]   Mocellin, S. (2009) Nitric Oxide: Cancer Target or Anti-cancer Agent? Current Cancer Drug Targets, 9, 214-236.
http://dx.doi.org/10.2174/156800909787581015

[4]   Wink, D.A. and Mitchell, J.B. (1998) Chemical Biology of Nitric Oxide: Insights into Regulatory, Cytotoxic, and Cytoprotective Mechanisms of Nitric Oxide. Free Radical Biology Medicine, 25, 434-456.
http://dx.doi.org/10.1016/S0891-5849(98)00092-6

[5]   Morbidelli, L., Donnini, S. and Ziche, M. (2004) Role of Nitric Oxide in Tumor Angiogenesis. Cancer Treatment and Research, 117, 155-167.
http://dx.doi.org/10.1007/978-1-4419-8871-3_11

[6]   Prostovit, L.M., Adams, M.A., Lash, G.E., Heaton, J.P. and Graham, C.H. (2002) Oxygen-Mediated Regulation of Tumor Cell Invasiveness. Involvement of a Nitric Oxide Signaling Pathway. Journal of Biological Chemistry, 277, 35730-35737.
http://dx.doi.org/10.1074/jbc.M204529200

[7]   Sanina, N.А. and Аldoshin, S.М. (2011) Structure and Properties of Iron Nitrosyl Complexes with Functionalized Sulfur-Containing Ligands. Russian Chemical Bulletin, International Edition, 60, 1223-1251.
http://dx.doi.org/10.1007/s11172-011-0192-x

[8]   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

[9]   Sanina, N.A., Syrtsova, L.A., Shkondina, N.I., Malkova, E.S., Kotelnikov, A.I. and Aldoshin, S.M. (2007) Hemoglobin-Stabilized Tetranitrosyl Binuclear Iron Complex with Pyridine-2-yl in Aqueus Solutions. Russian Chemical Bulletin, International Edition, 56, 761-766.
http://dx.doi.org/10.1007/s11172-007-0114-0

[10]   Roudneva, T.N., Syrtsova, L.A., Sanina, N.A., Shkondina, N.I., Kotelnikov, A.I. and Aldoshin, S.M. (2010) Formation of Iron Nitrosyl Complexes of Ferri- and Ferrocytochrome C at Its Interaction with Nitrosyl Iron Complex Cysaconite. Nitric Oxide: Biology and Chemistry, 22, 546.

[11]   Arnone, A. (1972) X-Ray Diffraction Study of Binding of 2,3-Diphosphoglycerate to Human Deoxyhaemoglobin. Nature, 237, 146-149.
http://dx.doi.org/10.1038/237146a0

[12]   Sanina, N.A., Syrtsova, L.A., Psikha, B.L., Tukhvatullin, I.A., Shkondina, N.I., Rudneva, T.N., Kotel’nikov, A.I. and Aldoshin, S.M. (2012) Revealing of the Cation-Binding Sites on the Surface of Hemoglobin in Its Reaction with the NO Donor, the Nitrosyl Iron Complex {Fe2[S(CH2)2NH3]2(NO)4}SO4·2.5H2O. Russian Chemical Bulletin, 61, 2350-2355.
http://dx.doi.org/10.1007/s11172-012-0330-0

[13]   Sanina, N.A., Lysenko, K.A., Zhukova, O.S., Roudneva, T.N., Emel’yanova, N.S. and Aldoshin, S.M. (2011) Water-Soluble Binuclear Nitrosyl Iron Complexes with Natural Aliphatic Thiolyls Possessing Cytotoxic, Apoptotic and NO Donor Activity. Patent No. US 8, 067, 628 B2.

[14]   Roudneva, T.N., Sanina, N.A., Lyssenko, K.A., Aldoshin, S.M., Antipin, M.Y. and Ovanesyan, N.S. (2009) Synthesis and Structure of a Water-Soluble Nitrosyl Iron Complex with Cysteamine Ligand. Mendeleev Communications, 19, 253-255.
http://dx.doi.org/10.1016/j.mencom.2009.09.006

[15]   Sanina, N.A., Serebryakova, L.I., Shul’zhenko, N.S., Pisarenko, O.I., Roudeva, T.N. and Aldosin, S.M. (2012) Application of Iron Binuclear Complex Sulphur-Nitrosyl Complex of the Canionic Type as a Vasodilative Drug. Patent No. RU No 2460531 C1.

[16]   De Lano, W.L. (2002) The PyMOL Molecular Graphics System. Version 0.99rc6 Schrödinger, LLC, De Lano Scientific, San Carlos.

[17]   Perutz, M.F., Fermi, G., Poyart, C., Pagnier, J. and Kister, J. (1993) A Novel Allosteric Mechanism in Haemoglobin. Structure of Bovine Deoxyhaemoglobin, Absence of Specific Chloride-Binding Sites and Origin of the Chloride-Linked Bohr Effect in Bovine and Human Haemoglobin. Journal of Molecular Biology, 233, 536-545.
http://dx.doi.org/10.1006/jmbi.1993.1530

[18]   Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., Meyer Jr., E.F., Brice, M.D., Rodgers, J.R., Kennard, O., Shimanouchi, T. and Tasumi, M. (1977) The Protein Data Bank: A Computer-Based Archival File for Macromolecular Structures. Journal of Molecular Biology, 112, 535-542.
http://dx.doi.org/10.1016/S0022-2836(77)80200-3

[19]   Miles, A.M., Wink, D.A., Cook, J.C. and Grisham, M.B. (1996) Determination of Nitric Oxide Using Fluorescence Spectroscopy. In: Packer, L., Ed., Methods in Enzymology V, Part A, Academic Press, New York, 105-121.

[20]   Cassoly, R. and Gibson, Q.H. (1975) Conformation, Co-Operativity and Ligand Binding in Human Hemoglobin. Journal of Molecular Biology, 91, 301-313.
http://dx.doi.org/10.1016/0022-2836(75)90382-4

[21]   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.

[22]   Syrtsova, L.A., Sanina, N.A., Lyssenko, K.A., Kabachkov, E.N., Psikha, B.L., Shkondina, N.I., Pokidova, O.V., Kotelnikov, A.I. and Aldoshin, S.M. (2014) Reversible Dissociation and Ligand-Glutathione Exchange Reaction in Binuclear Cationic Tetranitrosyl Iron Complex with Penicillamine. Bioinorganic Chemistry and Applications, 2014, Article ID: 641407.
http://dx.doi.org/10.1155/2014/641407

[23]   Sanina, N.A. Syrtsova, L.A., Chudinova, E.S., Shkondina, N.I., Rudneva, T.N., Kotelrnikov, A.I. and Aldoshin, S.M. (2009) Regularities in the Stabilization by Hemoglobin of Binuclear Iron Complexes [Fe2(μ-N-C-SR)2(NO)4] Containing Benzimidazolyl and Benzothiazolylthiol Ligands. Russian Chemical Bulletin, 58, 566-571.

[24]   Haurowitz, F. and Hardin, R. (1954) Respiratory Proteins. In: Neurath, H. and Bailey, K., Eds., The Proteins, Academic Press, New York, 279-344.

[25]   Perutz, M.F., Shih, D.T. and Williamson, D. (1994) The Chloride Effect in Human Hemoglobin: A New Kind of Allosteric Mechanism. Journal of Molecular Biology, 239, 555-560.
http://dx.doi.org/10.1006/jmbi.1994.1394

 
 
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