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Myoglobin H2O2 reaction

As described above, efficient peroxidase catalysis requires rapid reaction of the enzyme with H2O2 coupled with the formation of a discrete compound I species. As initially observed by George and Irvine in 1952 (177), the reaction of metMb with H2O2 is much slower than the corresponding reaction of peroxidases. The myoglobin derivative produced by this reaction was referred to by these authors as ferryl myoglobin... [Pg.22]

This Fe(IV)-derivative is particularly stable with leghemoglobin, while with other hemoglobins and with myoglobins the oxy form is regenerated with H2O2 The reaction of sufficient concentrations of H Oj with methemoglobin could formally yield the OH radical ... [Pg.17]

Although both haemoglobin [155,231] and myoglobin produce ferryl iron and free radicals upon addition of H2O2, the latter reaction has been studied more extensively. In contrast to most peroxidases, at least two myoglobin-bound free radicals have been detected immediately after peroxide addition, both by room-temperature [142] and low-temperature EPR[137]. These decay rapidly and independently of the decay of the ferryl iron, which is stable for at least an hour. It is not necessary to add exogenous reductants to reduce the radicals it is possible that some of the electrons come from elsewhere on the protein as different, more stable, free radicals can be detected one hour subsequent to peroxide treatment [137,236]. [Pg.102]

Myoglobin, unlike cytochrome P450 , cytochrome c peroxidase, and horseradish peroxidase, normally functions as an oxygen transport protein rather than as an enzyme. However, the availability of an iron coordination site in the ferric and deoxy ferrous states makes possible a reaction between the hemoprotein and H2O2. This reaction produces a... [Pg.261]

Wilks and P.R. Ortiz de Montellano, Intramolecular translocation of the protein radical formed in the reaction of recombinant sperm whale myoglobin with H2O2,/. Biol Chem. 267 8827 (1992). [Pg.265]


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Myoglobin

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