Proteomics of lipid oxidation‐induced oxidation of porcine and bovine oxymyoglobins

Suman, Surendranath P.; Faustman, C.; Stamer, Sheryl L.; Liebler, Daniel C.

doi:10.1002/pmic.200600313

Cited by 117 publications

(122 citation statements)

References 89 publications

Supporting

Mentioning

109

Contrasting

Unclassified

Order By: Relevance

“…Marcinek et al (2001) reported that the oxygen binding depends on the amino acid sequence surrounding the heme pocket. In addition, the primary amino acid sequence can affect the tertiary structure, which in turn can influence interaction with ligands and also the volume of the heme cavity (Suman et al, 2007). In support, Bunn (1971) reported that porcine hemoglobin has greater oxygen affinity than bovine hemoglobin, due to differences in amino acid composition.…”

Section: Discussionmentioning

confidence: 74%

“…In support, Bunn (1971) reported that porcine hemoglobin has greater oxygen affinity than bovine hemoglobin, due to differences in amino acid composition. Furthermore, variation in the primary structure was responsible for species-specific effects of secondary lipid oxidation products on myoglobin redox stability (Suman et al, 2007). For example, porcine myoglobin contains 9 histidine residues, while bovine myoglobin contains 13 residues.…”

Section: Discussionmentioning

confidence: 99%

“…More specifically, the number of histidine residues in the myoglobin of meat-producing livestock species can influence myoglobin redox stability (Suman et al, 2007). The amino acid composition can affect the 3-dimensional structure, hence the ability of heme to accept an electron or oxygen.…”

Section: Species-specificity In Myoglobin Oxygenation and Reduction Pmentioning

confidence: 99%

See 2 more Smart Citations

Species-Specificity in Myoglobin Oxygenation and Reduction Potential Properties

Nerimetla

Krishnan

Mazumder

et al. 2017

Meat and Muscle Biology

View full text Add to dashboard Cite

Abstract:The objective was to compare oxygenation and reduction potential properties of bovine and porcine myoglobins in-vitro. Cyclic voltammetry and homology-based myoglobin modeling were used to determine the species-specific effects on myoglobin reduction potential and oxygenation properties at pH 5.6, 6.4, and 7.4. At all pHs, porcine myoglobin had greater (P = 0.04) oxygen affinity than bovine myoglobin. For both species, oxygen affinity was higher at pH 6.4 > pH 7.4 > 5.6 (P = 0.0002). Myoglobin reduction potential for both species was affected by pH (P < 0.0001). The redox potentials became more negative as pH increased, indicating a proton-coupled electron transfer. There were no differences (P = 0.51) between species in reduction potential properties of heme. Homology-based myoglobin modeling indicated that the porcine myoglobin has a shorter distance between the distal histidine and heme than does bovine myoglobin. The variation in amino acid composition between bovine and porcine myoglobin could be partially responsible for differences in oxygen affinity.

show abstract

Section: Discussionmentioning

confidence: 74%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Species-Specificity in Myoglobin Oxygenation and Reduction Potential Properties

Nerimetla

Krishnan

Mazumder

et al. 2017

Meat and Muscle Biology

View full text Add to dashboard Cite

show abstract

“…Mammalian O 2 (II)Mb can be oxidized by copper ions with a dependence on binding of the metal to histidine residues in a species (pig, sperm whale, and horse)-specific manner (44). The lipid oxidation product, 4-hydroxy-2-nonenal (HNE), binds to His 24, 36, and 119 in pig Mb and His 24, 36, 81, 88, 93, 119, and 152 in bovine Mb (71). HNE binding to Mb has been shown to accelerate Mb oxidation.…”

Section: Reactions Of Mb With Other Biomoleculesmentioning

confidence: 99%

Redox Reactions of Myoglobin

Richards

2013

Antioxidants & Redox Signaling

View full text Add to dashboard Cite

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.

show abstract

“…The mechanism responsible for Mb aggregation has been partly characterized; Mb itself tends to self-aggregate (Chow et al, 1989), whereas it has been reported that, in postmortem meat, Mb binds to myofibrillar proteins (Chajian et al, 2008) or reacts with fatty acids (Suman et al, 2007).…”

Section: Resultsmentioning

confidence: 99%

Assessment of Commercial Quality Evaluation of Yellowfin Tuna Thunnus albacares Meat Based on Myoglobin Properties

Nurilmala

Ushio

Kaneko

et al. 2013

FSTR

View full text Add to dashboard Cite

Four quality grades (excellent, good, acceptable, and "not acceptable") of yellowfin tuna meat (Thunnus albacares), as judged by a professional appraiser, were compared based on the red/ox state and extractability of myoglobin (Mb). As a result, the metMb ratio of the "not acceptable" grade of meat was significantly higher than that of the other higher-grade samples. In contrast, the highest ratio of oxyMb was found in the "excellent" meat, followed by good > acceptable > "not acceptable" meats. Color measurement revealed significant differences in a* value between the different grades of meat, but showed essentially no difference in L* and b* values. Both a* value and redness index (a*/b*) showed high correlation coefficients with metMb ratio. Mb extractability tended to be higher in the higher grade of meat. In conclusion, the commercial appraisal of tuna meat quality was demonstrated to be reliable. Keywords: tuna, meat, quality, color, myoglobin *To whom correspondence should be addressed. E-mail: aochiai@tokai-u.jp IntroductionSeven species of tunas are consumed around the world. Yellowfin tuna (Thunnus albacores), whose meat is characterized by a light red color and less fat, is one of the most commercially important and favored tuna species. This scombridae species inhabits tropical and subtropical waters around the world. Therefore, this species is generally exported to Japan from tropical countries, such as Indonesia, Taiwan, and so on (MMAF, 2012). A quality check is frequently performed before processing and transportation. Sensory analyses performed by experienced appraisers are generally carried out to determine freshness as a composite of qualitative traits. Color is one of the most important factors affecting consumer preferences. The meat color of tuna is closely related with myoglobin (Mb) content and the red/ox state of the heme iron.Mb is a small globular protein whose biological function is basically to temporarily store oxygen in skeletal and cardiac muscles for facilitation of respiration (Livingston et al., 1983), though new functions of Mb have been recently reported, such as nitrogen oxide scavenging activity (Cossins and Berenbrink, 2008;Flögel et al., 2010;Helbo et al., 2012). Generally, Mb content changes dependent on animal species, muscle part, age, and diet of the animal. Pale colored meat, such as chicken and pork, generally contain lower concentrations of Mb compared with red colored meat such as beef. Oxidative muscles, namely, slow skeletal muscle (including the dark muscle of fish) and heart muscle, contain abundant Mb. In scombridae fish such as tuna, abundant Mb is also found in fast skeletal muscle (also referred to as ordinary muscle, light muscle or white muscle).An iron atom of heme is placed in the hydrophobic region of Mb, binding the imidazole group of proximal histidine directly and distal histidine through a coordinate bond (Phillips and Schoenboen, 1981). The binding of oxygen, as well as the state of an iron atom in the heme pocket, contributes to the meat colo...

show abstract

Proteomics of lipid oxidation‐induced oxidation of porcine and bovine oxymyoglobins

Cited by 117 publications

References 89 publications

Species-Specificity in Myoglobin Oxygenation and Reduction Potential Properties

Species-Specificity in Myoglobin Oxygenation and Reduction Potential Properties

Redox Reactions of Myoglobin

Assessment of Commercial Quality Evaluation of Yellowfin Tuna Thunnus albacares Meat Based on Myoglobin Properties

Contact Info

Product

Resources

About