Concentration effects in myoglobin-catalyzed peroxidation of linoleate

Caroline P. Baron, Leif H. Skibsted, Henrik J. Andersen

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The concentration of the free fatty acid anion linoleate was found to be important for the pro-oxidative activity of metmyoglobin, MbFe(III), and for mixtures of metmyoglobin and hydrogen peroxide, MbFe(III)/H2O2, to yield perferrylmyoglobin, *MbFe(IV)=O, whereas for ferrylmyoglobin, MbFe(IV)=O, no concentration effect was noted as studied in linoleate emulsions (pH 7.4 and 25 degreesC). Determination of conjugated dienes using second-derivative absorption spectroscopy, changes in Soret band absorbance, and spin-trapping ESR spectroscopy with alpha-(4-pyridyl-1-oxide)-N-tert-butyl nitrone (POBN) as the spin trap were used to evaluate the pro-oxidative activity of myoglobins. At a linoleate (LA)/heme protein (HP) ratio of 100, no MbFe(III)-induced linoleate peroxidation was observed, as MbFe(III) was converted to its non-pro-oxidative low-spin derivative, hemichrome, independently of the presence of H2O2. At higher LAMP ratios, linoleate peroxidation was initiated by the addition of MbFe(III), both in the presence and in the absence of H2O2. This proceeded with denaturation of MbFe(III), as followed by changes in Soret absorption band, which most probably release or expose the heme group to the environment and thereby permit hematin-induced lipid peroxidation. The obtained results show that the mechanism by which MbFe(IV)=O initiates linoleate peroxidation is different from MbFe(III)- and MbFe(III)/H2O2-initiated linoleate peroxidation. The shift in mechanism between heme protein cleavage of lipid hydroperoxides and hematin-induced lipid peroxidation is discussed in relation to oxidative progress in biological systems and muscle-based foods.
Original languageEnglish
JournalJournal of Agricultural and Food Chemistry
Volume50
Issue number4
Pages (from-to)883-888
Number of pages6
ISSN0021-8561
DOIs
Publication statusPublished - 2002
Externally publishedYes

Keywords

  • Electron Spin Resonance Spectroscopy
  • Ferric Compounds
  • Hemeproteins
  • Hemin
  • Hydrogen Peroxide
  • Linoleic Acid
  • Lipid Peroxidation
  • Myoglobin
  • Oxidants
  • Spectrophotometry
  • hemichrome
  • 743LRP9S7N Hemin
  • 9KJL21T0QJ Linoleic Acid
  • BBX060AN9V Hydrogen Peroxide
  • alkadiene
  • fatty acid
  • ferric ion
  • ferrylmyoglobin
  • hematin
  • hemin
  • hemoprotein
  • hydrogen peroxide
  • hydroperoxide
  • linoleic acid
  • metmyoglobin
  • myoglobin
  • n tert butyl alpha (4 pyridyl 1 oxide) nitrone
  • oxidizing agent
  • absorption spectroscopy
  • article
  • catalysis
  • concentration response
  • electron spin resonance
  • emulsion
  • environment
  • lipid peroxidation
  • metabolism
  • peroxidation
  • protein degradation
  • spectrophotometry
  • Ferrylmyoglobin
  • Hematin
  • Heme degradation
  • Lipid peroxidation
  • Metmyoglobin
  • Perferrylmyoglobin
  • AGRICULTURE,
  • CHEMISTRY,
  • FOOD
  • DRY-CURED HAM
  • HYDROGEN-PEROXIDE
  • LIPID-PEROXIDATION
  • FATTY-ACIDS
  • OXIDATION
  • HEMOGLOBIN
  • METMYOGLOBIN
  • LIPOLYSIS
  • BINDING
  • HEME
  • perferrylmyoglobin
  • heme degradation
  • muscle-based foods meat product
  • conjugated dienes
  • hematin 15489-90-4
  • heme protein
  • hydrogen peroxide 7722-84-1
  • linoleate 1509-85-9 peroxidation
  • 10060, Biochemistry studies - General
  • 10064, Biochemistry studies - Proteins, peptides and amino acids
  • 10065, Biochemistry studies - Porphyrins and bile pigments
  • 13502, Food technology - General and methods
  • 13516, Food technology - Meats and meat by-products
  • Biochemistry and Molecular Biophysics
  • Foods
  • FATTY ACID ESTERS
  • H2O2
  • HAEM
  • HAEMATIN
  • HETEROCYCLIC COMPOUNDS
  • LINOLEATES
  • MYOGLOBIN
  • ORGANIC NITROGEN COMPOUNDS
  • PEROXIDATION
  • PEROXIDES
  • PIGMENTS
  • PRESERVATIVES
  • Chemistry and biochemistry
  • Food sciences

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