Myoglobin and haemoglobin-mediated lipid oxidation in washed muscle: Observations on crosslinking, ferryl formation, porphyrin degradation, and haemin loss rate

Lee, Sung Ki; Tatiyaborworntham, Nantawat; Grunwald, Eric W.; Richards, Mark

doi:10.1016/j.foodchem.2014.06.098

Cited by 34 publications

(33 citation statements)

References 35 publications

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“…In the absence of GdnHCl, unfolding leads to aggregation of the unfolded globin states (UH, U), making the process irreversible. Any released free hemin is highly toxic in vivo where it partitions into membranes and promotes lipid oxidation and generation of reactive oxygen species (7)(8)(9)(10).…”

Section: Myoglobin (Mb)mentioning

confidence: 99%

Apoglobin Stability Is the Major Factor Governing both Cell-free and in Vivo Expression of Holomyoglobin

Samuel

Smith

Phillips

et al. 2015

Journal of Biological Chemistry

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Background: Myoglobin expression is highly variable in animal tissues and in E. coli. Results: The parameters governing holomyoglobin expression were determined experimentally. Conclusion: Both cell-free and in vivo holomyoglobin yields depend quantitatively on the stability of apoglobin and not hemin affinity. Significance: Enhanced apomyoglobin stability is required for high levels of holoprotein expression due to rapid rates of aggregation of unfolded apoproteins.

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Section: Myoglobin (Mb)mentioning

confidence: 99%

Apoglobin Stability Is the Major Factor Governing both Cell-free and in Vivo Expression of Holomyoglobin

Samuel

Smith

Phillips

et al. 2015

Journal of Biological Chemistry

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“…Hemin loss was measured at 37 °C and pH 5.7 to ensure that an accurate rate of hemin release from metMb could be obtained. Lower temperature such as 4 °C result in such low rates of hemin loss from mammalian Mb (Lee and others ) that a hemin loss rate could not be determined accurately. Thus, 37 °C was used for hemin loss measurements from bovine metMb compared to bovine metHb.…”

Section: Resultsmentioning

confidence: 99%

“…MetHb and MetMb were prepared as described previously (Lee and others ). Briefly, 4 mol potassium ferricyanide was used to oxidize each mol of heme in Hb and Mb followed by elution using a 10DG desalting column (Bio‐Rad, Hercules, Calif., U.S.A.) to remove unreacted potassium ferricyanide.…”

Section: Methodsmentioning

confidence: 99%

“…Procedures used have been described previously (Lee and others ). Briefly, metHb and metMb were added separately to washed cod muscle and stored at 2 °C for 2 d. Lipid oxidation products were measured during storage as described below.…”

Section: Methodsmentioning

confidence: 99%

“…“Hemeˮ and “heminˮ are the terms to describe protoporphyrin IX containing an iron atom in the Fe 2+ and Fe 3+ state, respectively so that oxyHb, oxyMb, deoxyHb, and deoxyMb contain “hemeˮ while metHb and metMb contain “hemin.ˮ Heme loss rates are essentially negligible when examining reduced Hb and Mb whereas metHb has relatively low hemin affinity compared to metMb (Bunn and Jandl ; Gattoni and others ). When comparing different Mbs, hemin loss from fish metMb was shown to be 3‐fold higher compared to mammalian metMb at pH 5.5 and 4 °C yet no hemin loss was detected at pH 6.0 and 4 °C (Lee and others ). A pH decrease from 7.0 to 5.0 increased hemin loss rates 142‐fold in sperm whale metMb at 37 °C (Hargrove and others ).…”

Section: Introductionmentioning

confidence: 99%

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Assessing Low Redox Stability of Myoglobin Relative to Rapid Hemin Loss from Hemoglobin

Tatiyaborworntham

Yin

et al. 2015

Journal of Food Science

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Bovine myoglobin (Mb) auto-oxidized 11-fold faster at pH 5.7 compared to bovine hemoglobin (Hb). Replacement of Ser(F7) in bovine Mb with positively charged or large apolar residues decreased auto-oxidation rates (2- to 4-fold) in comparison with wild-type Mb (P < 0.05). However, the same substitutions increased hemin loss rate (15- to 28-fold), indicating that hydrogen bonding between Ser(F7) and the heme-7-propionate is critical for stabilizing protoporphyrin in the globin. The anchoring of Ser(F7) to the heme-7-propionate in the proximal pocket of Mb is suggested to expose the distal pocket to solvent molecules that accelerate auto-oxidation. The rate of hemin loss from metHb at pH 5.7 was 68-fold faster compared to metMb. The ability of Ser(F7) and His(FG3) in Mb to form stabilizing contacts with the heme-7-propionate maintains hemin within the globin whereas Leu(F7) and Leu(FG3) of Hb cannot form stabilizing contacts which results in low hemin affinity. MetHb promoted lipid oxidation more effectively in washed muscle at pH 5.7 compared to metMb (P < 0.05). The greater ability of bovine metHb to promote lipid oxidation is likely due to its enhanced rate of hemin dissociation compared to bovine metMb.

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Caffeic acid: an antioxidant with novel antisickling properties

et al. 2021

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It is well documented that caffeic acid (3,4‐dihydroxycinnamic acid) (CA) interacts with and inhibits the oxidative reactions of myoglobin (Mb) and hemoglobin (Hb), and this interaction underlies its antioxidative action in meat. Sickle cell hemoglobin (HbS) is known for its tendency to oxidize more readily than normal HbA in the presence of hydrogen peroxide (H2O2), which leads to a more persistent and highly oxidizing ferryl Hb (HbFe4+). We have investigated the effects of CA on HbS oxidation intermediates, specifically on the ferric/ferryl forms. At a low concentration of H2O2 (0.5‐fold over heme), we observed a fivefold reduction in the amount of HbFe4+ accumulated in a mixture of ferric and H2O2 solution. Higher levels of H2O2 (onefold and twofold over heme) led to a lesser threefold and twofold reduction in the content of HbFe4+, respectively, possibly due to the saturation of the binding sites on the Hb molecule. The most intriguing finding was that when 5‐molar excess CA over heme was used, and a considerable increase in the delay time of HbS polymerization to approximately 200 s was observed. This delay in polymerization of HbS is theoretically sufficient to avoid microcapillary blockage and prevent vasoconstrictions in vivo. Mass spectrometry analysis indicated that CA was more extensively covalently bonded to βCys93 than to βCys112 and αCys104. The dual antioxidant and antisickling properties of CA may be explored further to maximize its therapeutic potential in SCD.

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Myoglobin and haemoglobin-mediated lipid oxidation in washed muscle: Observations on crosslinking, ferryl formation, porphyrin degradation, and haemin loss rate

Cited by 34 publications

References 35 publications

Apoglobin Stability Is the Major Factor Governing both Cell-free and in Vivo Expression of Holomyoglobin

Apoglobin Stability Is the Major Factor Governing both Cell-free and in Vivo Expression of Holomyoglobin

Assessing Low Redox Stability of Myoglobin Relative to Rapid Hemin Loss from Hemoglobin

Caffeic acid: an antioxidant with novel antisickling properties

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