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Декабрь 2014 (published: 03.12.2014)
Number 4(22)
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Stability of iron-porphyrin complexes red colo and properties of the ligand
Paramonova A.P., Murashev S.V.
Keywords: myoglobin, heme, porphyrin ring, iron ion, ligands, polarizability.
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
Stability of iron-porphyrin complexes red colo and properties of the ligand
Storing red fresh meat is largely dependent on the stability of a bright red pigment of muscle tissue - oxymyoglobin. The problem is that oxymyoglobin able to spontaneous autoxidation. The set of processes initiated by oxidation of the iron ion of the heme group is accompanied by generation of reactive oxygen species and hydroxyl ions. Free radicals can destroy the porphyrin ring of heme and thus even more change red meat. The formation of hydroxyl ions, the pH shifts to the alkaline side, which creates the necessary conditions for the growth of microorganisms. Microorganisms in turn also change the red color of meat and accelerate its deterioration. Thus, the stability of red meat is closely linked to long-term preservation of its freshness.
In this regard, requires identifying properties of a ligand capable of displacing oxygen in the heme myoglobin to form stable complexes with red iron-porphyrin.
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Read the full article
Keywords: myoglobin, heme, porphyrin ring, iron ion, ligands, polarizability.
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License