The reaction between metmyoglobin and hydrogen peroxide

George, Philip; Irvine, D. H.

doi:10.1042/bj0520511

Cited by 279 publications

(101 citation statements)

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“…The involvement of hydroxyl radicals was eliminated by the finding that high concentrations of mannitol did not inhibit the observed EPR signals [7]. Although these experiments have not eliminated a possible catalytic role for a higher oxidation state of metmyoglobin [ 18] in the N-demethylation of aminopyrine by cumene hydroperoxide, they have clearly demonstrated the existence of free radicals derived from the hydroperoxide which are capable of oxidizing aminopyrine. Similar studies of cytochrome P-450-dependent oxidations supported by cumene hydroperoxide are in progress.…”

Section: Ch3mentioning

confidence: 97%

Spin trapping evidence for free radical oxidants of aminopyrine in the metmyoglobin—cumene hydroperoxide system

Griffin

Ting

1978

FEBS Letters

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Section: Ch3mentioning

confidence: 97%

Spin trapping evidence for free radical oxidants of aminopyrine in the metmyoglobin—cumene hydroperoxide system

Griffin

Ting

1978

FEBS Letters

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“…First reported by George and Irvine in the 1950s, a green haem protein product was generated when metMb was reacted with H 2 O 2 at acidic pH values proposing that the green species was an irreversible oxidative modification to the haem porphyrin structure (26). 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.…”

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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“…In 1923, the peroxidase activity of Hb has been reported (19), and in 1938, the modulation of the peroxidase activity of Hb by haptoglobin has been demonstrated (20). The reaction of myoglobin (Mb) with H 2 O 2 , on the other hand, apparently was not considered until 1952 (21), and the ability of Mb to catalyze peroxide oxidation of substrates was not reported until 1955 (22). Upon reaction with H 2 O 2 , Mb and Hb form the cytotoxic ferryl derivative (heme-Fe(IV)¼ ¼O), which is similar to compound II formed by peroxidases (23,24).…”

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confidence: 99%

Catalytic peroxidation of nitrogen monoxide and peroxynitrite by globins

et al. 2008

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SummaryGlobins are generally considered as carriers of diatomic gaseous ligands (e.g., O 2 and NO) in metazoa. Recently, the (pseudo-)enzymatic activity of globins towards reactive nitrogen and oxygen species has been elucidated. In particular, some globins (e.g., hemoglobin and myoglobin) catalyze the enzymatic scavenging of NO and peroxynitrite in the presence of H 2 O 2 . Indeed, H 2 O 2 oxidizes some globins leading to the formation of water and of the heme-protein ferryl derivative, which, in turn, oxidizes NO and peroxynitrite leading to the formation of the globin ferric species, NO 2 2 , and NO 3 2 . Here, we hypothesize that NO, peroxynitrite, and H 2 O 2 are co-substrates for the peroxidase activity of some globins, this catalytic activity was reported in 1900 for the first time, even though the substrates have never been identified firmly up to now. The hemoglobin (Hb) superfamily includes several hemeproteins, generally referred to as globins, which are found in all kingdoms of living organisms (1, 2). Globin functions have been the subject of active debate, in addition to dioxygen transport and storage. Several functions have been proposed recently, including control of nitrogen monoxide levels, O 2 sensing, and dehaloperoxidase activity (3-15).Globins share physical, spectroscopic, and chemical similarities with peroxidases (16,17). In fact, as demonstrated first in 1900 (18), Hb reacts readily with hydrogen peroxide (H 2 O 2 ). In 1923, the peroxidase activity of Hb has been reported (19), and in 1938, the modulation of the peroxidase activity of Hb by haptoglobin has been demonstrated (20). The reaction of myoglobin (Mb) with H 2 O 2 , on the other hand, apparently was not considered until 1952 (21), and the ability of Mb to catalyze peroxide oxidation of substrates was not reported until 1955 (22). Upon reaction with H 2 O 2 , Mb and Hb form the cytotoxic ferryl derivative (heme-Fe(IV)¼ ¼O), which is similar to compound II formed by peroxidases (23, 24). Heme-Fe(IV)¼ ¼O is able to oxidize a wide range of reducing substrates, such as phenols and aromatic amines, even though substrate peroxidation by Hb and Mb is far less efficient than that of peroxidases (24, 25), ruling out the possibility that the potential peroxidase activity of Hb and Mb is exerted on this class of substrates under normal conditions.Here, we hypothesize that the capability of some globins (e.g., Hb and Mb) to form a compound II-like species under oxidative stress may be actually exploited to avoid the building up of NO and peroxynitrite, 1 which can be then identified as the 'true' substrates for the peroxidase activity of Hb and Mb.Heme-proteins share the ability of detoxifying nitrogen reactive species, for example, NO. Even though leukocyte peroxi- 1 The term peroxynitrite is used in the text to refer generically to both ONOO 2 and its conjugated acid HOONO (38).

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The reaction between metmyoglobin and hydrogen peroxide

Cited by 279 publications

References 5 publications

Spin trapping evidence for free radical oxidants of aminopyrine in the metmyoglobin—cumene hydroperoxide system

Spin trapping evidence for free radical oxidants of aminopyrine in the metmyoglobin—cumene hydroperoxide system

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

Catalytic peroxidation of nitrogen monoxide and peroxynitrite by globins

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