Interaction of Myoglobin Model with Ligands of Gas Exchange

V. A. Zavhorodnia, S. O. Kovalenko, B. F. Minaev

Abstract


Introduction. Gas exchange for living organisms is a very important biochemical process. Hemoglobin blood imioglobin plays a leading role in him, located in the muscle fibers.In the study of various indicators of the cardiovascular and respiratory systems, the question arose about the competition of different gases for binding to Fe2+ haem haemoglobin.

Purpose. Until this time, nobody considered the possibility of binding of СО2 to iron of haemoglobin. For the first time, we have taken an attempt to consider this connection.

Methods. Calculations were made using ZINDO / 1 and PM3 methods in the HyperChem program.

Results. The issue of gas exchange with participation of haemoglobin is discussed. The potential curves of haem iron binding with CO, СО2 and О2 gases are calculated. The possibility of forming a complex for the haem model with carbon (IV) oxide is shown for the first time. The role of the upper occupied MO of iron-phosphorus and ligand in the formation of coordination bonds and charge transfer in the complex of haem with СО2 is determined. The role of charge polarization in the haem model is considered comparing СО2 with other gases.

Conclusion. Our quantum-chemical calculations show that СО2 can be coordinated with the iron ion in haemoglobin, although its binding energy is significantly less than that for the CO complex with haemoglobin and is about 34.5 kcal / mol.


Keywords


haemoglobin; myoglobin; carbon (IV) oxide; CO; О2; molecular orbitals; iron-porphyrin

References


Zinchuk V.V., Stepura T.L. (2016). NO-dependent mechanisms of intra-peritocitric regulation of the af finity of hemoglobin to oxygen: a monograph. GrGMU: Grodno. 176 (in Rus ).

Anderson W.P., Edwards W.D., Zerner M.C. (1986). Calculated spectra of hydrated ions of the first transition-metal series. Inorganic chemistry, 25, 2728-2732. DOI: 10.1021 / ic00236a015

Franzen S. (2002). Spin-dependent mechanism for diatomic ligand binding to heme. Proceeding of the National Academy of Sciences of the United States of America, 26, 16754–16759. www.pnas.org/cgi/doi/10.1073/pnas.252590999

Minaev B.P., Minaeva V.O., Obushko O.M., Govorun D.M. (2009). Investigation of models of oxygen binding by hemum using density functional. Biopolimery i klityna [Biopolymers and cell], 4, 298-330 (in Ukr). http://dx.doi.org/10.7124/bc.0007E9

Dudok K., Bilyi R., Fedorovich A. (2002). Research of ligand forms of hemoglobin by the method of electronic optical spectroscopy. Visnyk Lvivskoho universytetu [News of Lviv University], 29, 32-38 (in Ukr).

Pilkevich N. B., Razaybedin V.M., Boyarchuk O.D. (2007). Hemoglobin: structure, biochemistry and pathology: a manual for students in higher education. Lugansk: Alma mater, 90 (in Ukr).

Romanova T. A., Krasnov P. O., Avramov P.V. (2001). The electronic structure of hemoglobin complexes with ligands and dynamics of their atomic core at physiological temperature. Yssledovano v Rossyy [Investigated in Russia], 70, 781-791 (in Rus ).

Takashi Yonetani, SungIck Park, Antonio Tsuneshige, Kiyohiro Imai, Kenji Kanaori. (2002). Global Allostery Model of Hemoglobin. Modulation of O2 affinity, cooperativity, and bohr effect by heterotropic allosteric effectors. The American Society for Biochemistry and Molecular Biology. 2002. 1-52.

doi: 10.1074/jbc.M203135200

Minaev B.F. (2009). Spin-catalysis in photocatalysis and bioactivation processes of molecular oxygen. Ukrainskyi biokhimichnyi zhurnal [Ukrainian biochemical journal], 3, 21-45 (in Rus ).

Lepeshkevich S.V., Poznyak A.L., Dzhagarov B.M. (2005). Influence of zinc ions on the geminal and bimolecular stages of the oxygenation reaction of myoglobin horse. Zhurnal prykladnoi spektroskopii [Journal of Applied Spectroscopy], 5, 670-677 (in Rus ).

Sergunova V.A., Manchenko E.A., Gudkova O.E. (2016). Hemoglobin: modifications, crystallization, polymerization (review).Obshchaia reanymatolohyia [General reanimatology], 12 (6), 49-63 (in Rus ). doi: 10.15360/1813-9779-2016-6-49-63

Lepeshkevich C.V., Gilevich S.N., Parhots M.V., Dzhagarov B.M. (2016). Migration of molecular oxygen and carbon monoxide through xenon sites in isolated human hemoglobin chains. Еlektronna biblioteka derzhavnoho biloruskoho universytetu [Electronic Library of the State Belarusian University], 120-122 (in Rus ).

Nienhaus K., John S. Olson, Stefan Franzen, G. Ulrich Nienhaus. (2005). The Origin of Stark Splitting in the Initial Photoproduct State of MbCO. Journal of the American chemical society, 127 (1), 40-41 doi: 10.1021/ja0466917

De Angelis F., Andrzej A. Jarzȩcki, Roberto Car, Thomas G. Spiro. (2005) Quantum chemical evaluation of protein control over heme ligation: CO/O2 discrimination in myoglobin. Journal Physical Chemistry B, 109 (7), 3065–3070. doi: 10.1021/jp0451851

Tolkach P.G., Basharin V.A., Grebenyuk A.N. (2014). Mechanisms of neurotoxic action of carbon monoxide (review of literature). Byomedytsynskyi zhurnal [Biomedical Journal], 15, 142-154 (in Rus).

Fatkulin K.V., Gilmanov A.Zh., Kostyukov D.V. (2014). Clinical significance and modern methodological aspects of determining the level of carboxy of methemoglobin in the blood. Рraktycheskaia medytsyna [Practical medicine], 3 (79), 17-21 (in Rus ).

Drogovoz S.M., Strigol S. Yu., Kononenko A.V., Zupanets M.V., Levinskaya Ye.V. (2016). Physiological properties of CO2 - a rationale for the uniqueness of carboxytherapy. Medychna ta klinichna khimiia [Medical and Clinical Chemistry], 1, 112-116 (in Rus ). doi :10.11603 / mcch.2410-681X.2016.v0.i1.6203

Drogovoz S. M., Strigol S. Yu., Kononenko A.V., Zupanets M.V., Shtroblya A.L. (2016). Mechanism of action of carboxytherapy. Farmakolohiia ta likarska toksykolohiia [Pharmacology and drug toxicology], 6 (51), 12-20 (in Rus ). doi: https://doi.org/10.24959/ubphj.18.192

Artyukhov V.G., Putintseva O.V., Kalayeva E.A., Savostin V.С. (2015). Human hemoglobin under the influence of various physical and chemical agents (monograph). Mezhdunarodnыi zhurnal эksperymentalnoho obrazovanyia [International Journal of Experimental Education], 10, 113-115 (in Rus).

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