Multiple wavelength analysis of the reaction between hydrogen peroxide and metmyoglobin

Fox, Jay B.; Nicholas, Rosemary A.; Ackerman, S. A.; Swift, C. E.

doi:10.1021/bi00722a020

Cited by 76 publications

(50 citation statements)

References 19 publications

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“…The relative amount of the two products produced depends upon the pH of the solution. The simplest way to express the reaction sequence (Fox et al, 1974) can be given as where HMb and Mb are the protonated and deprotonated forms of myoglobin, respectively. The following equation can be derived from the above mechanism…”

Section: Resultsmentioning

confidence: 99%

The role of distal histidine in peroxidase activity of myoglobin

Khan

Mondal

Padhy

et al. 1998

European Journal of Biochemistry

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The distal histidine has been proposed to play a crucial role in the reaction of peroxidases with hydroperoxide. Myoglobin (Mb), due to its close similarity with peroxidases, also reacts with various peroxides. The effect of mutation of the distal histidine on the peroxidase activity of Mb has been investigated by stopped-flow kinetics of the reaction of hydrogen peroxide with wild-type Mb and [Gly64]Mb. The results indicate kinetic and mechanistic differences in the formation of peroxide compounds from these two forms of Mb. The rate of reaction of H 2 O 2 with the wild-type Mb decreased 8Ϫ9-fold on mutation of the distal histidine to glycine ([Gly64]Mb). A second slow phase was observed for the reaction of H 2 O 2 with [Gly64]Mb, but was not observed in the corresponding reaction with wild-type Mb. It is suggested that the decrease in the rate of the reaction on mutation is due to the absence of a general acid-base catalyst. The effect of pH on the rate of reaction of H 2 O 2 with wild-type Mb and [Gly64]Mb is contrasting. While the rate of the M6 reaction decreased for wild-type Mb at higher pH, probably due to the acid-alkaline transition of Mb at higher pH, the rate of reaction was found to increase at higher pH for mutant Mb. The increase in the rate of the reaction is suggested to be due to an increase in the ionization of H 2 O 2 at higher pH, the rate-determining step being the formation of the intermediate Fe-O-O-H complex and not the subsequent step of oxo-ferryl complex formation. The thermodynamic parameters calculated from the temperature-dependent study showed that the enthalpy of binding of H 2 O 2 with Mb is positive, indicating that the process is endothermic. The apparent energy of activation of the reaction of H 2 O 2 with Mb was found to be higher than that of peroxidases, suggesting that this may be oue of the reasons for the slower rate of the reaction of H 2 O 2 with Mb compared with peroxidases.

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Section: Resultsmentioning

confidence: 99%

The role of distal histidine in peroxidase activity of myoglobin

Khan

Mondal

Padhy

et al. 1998

European Journal of Biochemistry

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“…In 1974 Fox et al noted that this green product could not be separated from the protein by an acid solvent extraction method (27) and proposed that a proportion of the green haem was covalently attached to the protein. This hypothesis was confirmed in 1989 when the mechanism of haem to protein cross-linking was examined in detail (28).…”

Section: Introductionmentioning

confidence: 99%

Histidine and not tyrosine is required for the Peroxide‐induced formation of haem to protein cross‐linked myoglobin

et al. 2007

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SummaryPeroxide-induced oxidative modifications of haem proteins such as myoglobin and haemoglobin can lead to the formation of a covalent bond between the haem and globin. These haem to protein cross-linked forms of myoglobin and haemoglobin are cytotoxic and have been identified in pathological conditions in vivo. An understanding of the mechanism of haem to protein cross-link formation could provide important information on the mechanisms of the oxidative processes that lead to pathological complications associated with the formation of these altered myoglobins and haemoglobins. We have re-examined the mechanism of the formation of haem to protein cross-link to test the previously reported hypothesis that the haem forms a covalent bond to the protein via the tyrosine 103 residue (Catalano, C. E., Choe, Y. S., Ortiz de Montellano, P. R., J. Biol. Chem. 1989, 10534 -10541).Comparison of native horse myoglobin, recombinant sperm whale myoglobin and Tyr 103 ! Phe sperm whale mutant shows that, contrary to the previously proposed mechanism of haem to protein cross-link formation, the absence of tyrosine 103 has no impact on the formation of haem to protein cross-links. In contrast, we have found that engineered myoglobins that lack the distal histidine residue either cannot generate haem to protein cross-links or show greatly suppressed levels of modified protein. Moreover, addition of a distal histidine to myoglobin from Aplysia limacina, that naturally lacks this histidine, restores the haem protein's capacity to generate haem to protein cross-links. The distal histidine is, therefore, vital for the formation of haem to protein cross-link and we explore this outcome. IUBMB Life, 59: 477-489, 2007

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“…The peroxidative activity of methemoglobin and metmyoglobin has been well studied (8)(9)(10)(21)(22)(23)(24). It was first suggested by George and Irvine (8) that the reaction between metmyoglobin and H202 might produce OH'.…”

Section: Hemoglobin Autoxidatiormentioning

confidence: 99%

“…They observed ferrylmyoglobin as a product, a metmyoglobin:H202 stoichiometry of approximately 1:1, and evidence of a short-lived reactive intermediate. However, it was subsequently shown that the intermediate is equivalent to an Hb3"H202 complex, with one oxidizing equivalent located on the heme (ferryl) and one on the globin, i.e., giving a ferrylheme-globin radical (9,10). The radical nature ofthis species has been observed by ESR spectroscopy, with both hemoglobin and myoglobin (23)(24)(25).…”

Section: Hemoglobin Autoxidatiormentioning

confidence: 99%

“…This is thought to occur through internal peroxidation by Hb3+H202. Ferrylhemoglobin, represented as Fe4+, is equivalent to a Hb2'H202 complex (peroxidase compound II), although it appears to be unable to produce H202 by dissociation (8)(9)(10). Hb3+H202 refers to a short-lived ferryl radical internediate produced in the reaction ofmethemoglobin with H202 (9,10).…”

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confidence: 99%

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Free-radical production and oxidative reactions of hemoglobin.

Winterbourn¹

1985

Environ Health Perspect

153

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Mechanisms of autoxidation of hemoglobin, and its reactions with H2O2, O2-, and oxidizing or reducing xenobiotics are discussed. Reactive intermediates of such reactions can include drug free radicals, H2O2, and O2-, as well as peroxidatively active ferrylhemoglobin and methemoglobin-H2O2. The contributions of these species to hemoglobin denaturation and drug-induced hemolysis, and the actions of various protective agents, are considered.

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Multiple wavelength analysis of the reaction between hydrogen peroxide and metmyoglobin

Cited by 76 publications

References 19 publications

The role of distal histidine in peroxidase activity of myoglobin

The role of distal histidine in peroxidase activity of myoglobin

Histidine and not tyrosine is required for the Peroxide‐induced formation of haem to protein cross‐linked myoglobin

Free-radical production and oxidative reactions of hemoglobin.

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