Biochemistry (Moscow)

, Volume 81, Issue 13, pp 1735–1753 | Cite as

Hemoglobin and myoglobin as reducing agents in biological systems. Redox reactions of globins with copper and iron salts and complexes

  • G. B. PostnikovaEmail author
  • E. A. Shekhovtsova


In addition to reversible O2 binding, respiratory proteins of the globin family, hemoglobin (Hb) and myoglobin (Mb), participate in redox reactions with various metal complexes, including biologically significant ones, such as those of copper and iron. HbO2 and MbO2 are present in cells in large amounts and, as redox agents, can contribute to maintaining cell redox state and resisting oxidative stress. Divalent copper complexes with high redox potentials (E 0, 200-600 mV) and high stability constants, such as [Cu(phen)2]2+, [Cu(dmphen)2]2+, and CuDTA oxidize ferrous heme proteins by the simple outer-sphere electron transfer mechanism through overlapping π-orbitals of the heme and the copper complex. Weaker oxidants, such as Cu2+, CuEDTA, CuNTA, CuCit, CuATP, and CuHis (E 0≤ 100-150 mV) react with HbO2 and MbO2 through preliminary binding to the protein with substitution of the metal ligands with protein groups and subsequent intramolecular electron transfer in the complex (the site-specific outer-sphere electron transfer mechanism). Oxidation of HbO2 and MbO2 by potassium ferricyanide and Fe(3) complexes with NTA, EDTA, CDTA, ATP, 2,3-DPG, citrate, and pyrophosphate PPi proceeds mainly through the simple outer-sphere electron transfer mechanism via the exposed heme edge. According to Marcus theory, the rate of this reaction correlates with the difference in redox potentials of the reagents and their self-exchange rates. For charged reagents, the reaction may be preceded by their nonspecific binding to the protein due to electrostatic interactions. The reactions of LbO2 with carboxylate Fe complexes, unlike its reactions with ferricyanide, occur via the site-specific outer-sphere electron transfer mechanism, even though the same reagents oxidize structurally similar MbO2 and cytochrome b 5 via the simple outer-sphere electron transfer mechanism. Of particular biological interest is HbO2 and MbO2 transformation into met-forms in the presence of small amounts of metal ions or complexes (catalysis), which, until recently, had been demonstrated only for copper compounds with intermediate redox potentials. The main contribution to the reaction rate comes from copper binding to the “inner” histidines, His97 (0.66 nm from the heme) that forms a hydrogen bond with the heme propionate COO group, and the distal His64. The affinity of both histidines for copper is much lower than that of the surface histidines residues, and they are inaccessible for modification with chemical reagents. However, it was found recently that the high-potential Fe(3) complex, potassium ferricyanide (400 mV), at a 5 to 20% of molar protein concentration can be an efficient catalyst of MbO2 oxidation into metMb. The catalytic process includes binding of ferrocyanide anion in the region of the His119 residue due to the presence there of a large positive local electrostatic potential and existence of a “pocket” formed by Lys16, Ala19, Asp20, and Arg118 that is sufficient to accommodate [Fe(CN)6]4–. Fast, proton-assisted reoxidation of the bound ferrocyanide by oxygen (which is required for completion of the catalytic cycle), unlike slow [Fe(CN)6]4– oxidation in solution, is provided by the optimal location of neighboring protonated His113 and His116, as it occurs in the enzyme active site.


hemoglobin myoglobin leghemoglobin copper and iron salts and complexes redox reactions electrostatic potential 















metmyoglobin carboxyamidated at histidine residues


trans-1,2-diaminocyclohexane-N,N,N′,N′-tetraacetic acid




metmyoglobin carboxymethylated at histidine residues








ethylenediaminetetraacetic acid


electrostatic potential


nitrilotriacetic acid






reactive oxygen species


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© Pleiades Publishing, Ltd. 2016

Authors and Affiliations

  1. 1.Institute of Cell BiophysicsRussian Academy of SciencesPushchino, Moscow RegionRussia

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