Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin

Kanner, Joseph; Harel, Stella

doi:10.1016/0003-9861(85)90282-6

Cited by 366 publications

(219 citation statements)

References 46 publications

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“…1). With this hemoprotein, a high initial rate was also observed in the case of sarcosome peroxidation (14). Molar ratios for H202:leghemoglobin of 5 or 10 produced greater amounts of MDA.…”

Section: Peroxidation Of the Peribacteroid Membrane In The Presence Omentioning

confidence: 66%

“…826 gestions that iron-oxygen species are responsible for this initiation: perferryl radicals and specific Fe2+-Fe3+-O2 complexes have been considered (20). On the other hand, it has been proposed that ferryl species might account for the ability of mixtures of heme proteins and H202 to stimulate lipid peroxidation; thus, initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin has been reported (14). Leghemoglobin, a cytosolic myoglobin-like hemoprotein, is present in large quantities around the peribacteroid vesicles in the central tissue of nitrogen-fixing root nodules (1).…”

mentioning

confidence: 99%

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Lipid Peroxidation in Peribacteroid Membranes from French-Bean Nodules

Puppo¹,

Herrada²,

Rigaud³

1991

Plant Physiol.

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Enriched peribacteroid membranes were prepared from Phaseolus vulgaris nodules and, in the presence of metleghemoglobin and H202, membranal lipid peroxidation was observed. The initial rate of the reaction was low and increased with time. Ferrous leghemoglobin was unable to induce this peroxidation with H202. Thus, it appears that leghemoglobin (IV) is not the activated species involved in this process. Heme plays a role in this peroxidation and the hydroxyl radical is not an intermediate of the reaction. Lipid peroxidation in peribacteroid membranes was also observed in the presence of iron ions. A mixture of iron (Ill) and iron (II) produced a maximal peroxidation. Senescing nodule extracts were able to provoke membranal lipid peroxidation; they contained nonprotein-bound iron. Peribacteroid membranes were more sensitive than microsomes to peroxidation, as measured by malonaldehyde formation.

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Section: Peroxidation Of the Peribacteroid Membrane In The Presence Omentioning

confidence: 66%

mentioning

confidence: 99%

Lipid Peroxidation in Peribacteroid Membranes from French-Bean Nodules

Puppo¹,

Herrada²,

Rigaud³

1991

Plant Physiol.

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“…Mb + (IV) = O and Mb (IV) = O can abstract a hydrogen atom from polyunsaturated fatty acids (LH), which is an initiating step of lipid oxidation (35):…”

Section: Reactions Of Mb With Other Biomoleculesmentioning

confidence: 99%

Redox Reactions of Myoglobin

Richards

2013

Antioxidants & Redox Signaling

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Significance: Failure to maintain myoglobin (Mb) in the reduced state causes the formation of metMb, ferryl Mb species, and cross-linked Mb. Dissociation of ferriprotoporphyrin IX from the globin and release of iron atoms can also occur as oxidized Mb accumulates. These modifications may contribute to various oxidative pathologies in muscle and muscle foods. Recent Advances: The mechanism of ferryl Mb-mediated oxidative damage to nearby structures has been partially elucidated. Dissociation of ferriprotoporphyrin IX from metMb occurs more readily at acidic pH values. The dissociated ferriprotoporphyrin IX (also called hemin) readily decomposes preformed lipid hydroperoxides to reactive oxygen species. Heme oxygenase as well as lipophilic free radicals can degrade the protoporphyrin IX moiety, which results in the formation of free iron. Critical Issues: The multiple pathways by which Mb can incur toxicity create difficulties in determining the major cause of oxidative damage in a particular system. Peroxides and low pH activate each of the oxidative Mb forms, ferriprotoporphyrin IX, and released iron. Determining the relative concentration of these species is technically difficult, but essential to a complete understanding of oxidative pathology in muscle tissue. Future Directions: Improved methods to assess the different pathways of Mb toxicity are needed. Although significant advances have been made in the understanding of Mb interactions with other biomolecules, further investigation is needed to understand the physical and chemical nature of these interactions.

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“…The relationship between lipid oxidation and pigment oxidation is significant (Kanner & Harel 1985). Free radicals produced by lipid oxidation can initiate the reaction of oxidising oxymyoglobin to metmyoglobin.…”

mentioning

confidence: 99%

The effects of butylated hydroxyanisole, ascorbic acid, and α-tocopherol on some quality characteristics of mechanically deboned chicken patty during freeze storage

Ozgul¹,

Sarıçoban²

2010

Czech J. Food Sci.

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Ozer O., Sariçoban C. (2010): The effects of butylated hydroxyanisole, ascorbic acid, and α-tocopherol on some quality characteristics of mechanically deboned chicken patty during freeze storage. Czech J. Food Sci., 28: 150-160.In this study, the effects were evaluated of butylated hydroxyanisole (BHA), ascorbic acid (AA) and α-tocopherol (TO) on the stability of raw mechanically deboned chicken patties stored at -20°C for 6 months. pH, thiobarbituric acid reactive substance (TBARS), haem iron (mg/kg), metmyoglobin formation (%) and colour (L*, a*, b*, C* and h values) of patties were measured for 0, 2, 4, and 6 months of storage time. pH values were found to be the highest in the initial storage period. TBARS values were observed to range between 0.33 and 2.40 mg malondialdehyde/kg of sample and the L*, a*, and b* values of the patty samples during the storage period were found to range between 38.14 and 49.52, 9.01 and 20.87, and 7.28 and 14.62, respectively. The haem iron and metmyoglobin contents were found to range between 8.39 and 10.87 mg/kg and 19.26% and 45.91%, respectively. As a result, it is suggested that L-ascorbic acid and α-tocopherol can be added into chicken patty samples in view of the storage quality parameters mentioned above.

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Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin

Cited by 366 publications

References 46 publications

Lipid Peroxidation in Peribacteroid Membranes from French-Bean Nodules

Lipid Peroxidation in Peribacteroid Membranes from French-Bean Nodules

Redox Reactions of Myoglobin

The effects of butylated hydroxyanisole, ascorbic acid, and α-tocopherol on some quality characteristics of mechanically deboned chicken patty during freeze storage

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