Myoglobin oxidation

During the curing process, some of the nitrites are converted to nitric oxide. This combines with the myoglobin proteins in the muscle of the meat to form the deep red nitric oxide myoglobin, which causes cured meats such as ham to turn pink during the smoking process. 

Fig. 8.9 UV—Vis spectra of intercalated biomolecules assembled AMP. Soret band absorptions for (A) oxidized myoglobin (met-Mb) and after dithionite reduction (deoxy-Mb), and (B) after CO (CO-Mb) and 02 bindingto intercalated deoxy-Mb.

Mb. Subsequent application of this technique to reduction of various derivatives of reduced and oxidized myoglobin led to the observation that the rate of reduction by hydrated electrons depends primarily on the net charge of the protein and the dissociation constant for formation of ligand bound derivatives of metMb. 

Fox, J. B., and Ackerman, S. A. (1968). Formation of nitric oxide myoglobin Mechanisms of the reaction with various reductants. J. Food Set. 33, 364-370. 

Koizumi, C., and Brown, W. D. (1971). Formation of nitric oxide myoglobin by nicotinamide adenine dinucleotides and flavins. J. Food Sci. 36, 1105-1109. 

Reith, J. F., and Szakaly, M. (1967a). Formation and stability of nitric oxide myoglobin. 

Irwin, J. A., Ostdal, H., and Davies, M. J., Myoglobin-induced oxidative damage evidence for radical transfer from oxidized myoglobin to other proteins and antioxidants. Arch. Biochem. Biophys. 362, 94-104 (1999). 

Color stabilization by the addition of nitrate or nitrite (meat curing) plays an important role in meat processing. Nitrite initially oxidizes myoglobin to metmyoglobin ... 

The dissociation of carboxymyoglobin and nitric oxide myoglobin are described by similar expressions with smaller values for L. 

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