Related Experiment Video

Updated: Jul 28, 2026

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors
09:33

Imaging Approaches to Assessments of Toxicological Oxidative Stress Using Genetically-encoded Fluorogenic Sensors

Published on: February 7, 2018

Oxymyoglobin oxidation and membranal lipid peroxidation initiated by iron redox cycle

S Gorelik1, J Kanner

  • 1Department of Food Science, Institute for Technology and Storage of Agricultural Products, Agricultural Research Organization, P.O. Box 6, Bet Dagan 50250, Israel.

Journal of Agricultural and Food Chemistry
|December 18, 2001
PubMed

Insights

Oxymyoglobin oxidation, causing undesirable brown meat color, is accelerated by iron redox cycling. Higher oxymyoglobin concentrations can inhibit this oxidation and lipid peroxidation, suggesting a protective role.

Area of Science:

  • Food Science
  • Biochemistry
  • Meat Science

Background:

  • Oxymyoglobin is the primary pigment responsible for the red color in fresh meat.
  • Oxidation of oxymyoglobin to metmyoglobin results in a brown discoloration, which is undesirable for consumers.
  • Understanding the oxidation mechanism is crucial for maintaining meat quality.

Purpose of the Study:

  • To elucidate the mechanism of oxymyoglobin oxidation in muscle tissues.
  • To investigate the role of muscle membranes and an iron redox cycle in this process.
  • To determine the effects of varying concentrations of iron, ascorbic acid, and oxymyoglobin on oxidation rates.

Main Methods:

  • A model system using oxymyoglobin and muscle membranes was employed.
  • Oxymyoglobin oxidation was quantified by spectrophotometry at 582 nm.
  • Lipid peroxidation was assessed by measuring TBARS and conjugated dienes.

Main Results:

  • Ferric iron and low concentrations of ascorbic acid (200 microM) promoted both oxymyoglobin and lipid oxidation.
  • High concentrations of ascorbic acid (2000 microM) exhibited an antioxidative effect.
  • Increased oxymyoglobin concentrations (80 microM) significantly inhibited lipid peroxidation (>90%) and partially prevented oxymyoglobin oxidation.

Conclusions:

  • Iron redox cycling is a key driver of oxymyoglobin oxidation and associated meat browning.
  • Ascorbic acid's effect is concentration-dependent, acting as a pro-oxidant at low levels and an antioxidant at high levels.
  • Higher oxymyoglobin levels can offer protection against lipid peroxidation and self-oxidation, impacting meat stability.

More Related Videos

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases08:57

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases

Published on: February 24, 2018

Setup of Capillary Electrophoresis-Inductively Coupled Plasma Mass Spectrometry (CE-ICP-MS) for Quantification of Iron Redox Species (Fe(II), Fe(III))04:48

Setup of Capillary Electrophoresis-Inductively Coupled Plasma Mass Spectrometry (CE-ICP-MS) for Quantification of Iron Redox Species (Fe(II), Fe(III))

Published on: May 4, 2020

Related Concept Videos

Oxidation and Reduction of Organic Molecules01:19

Oxidation and Reduction of Organic Molecules

Energy production within a cell involves many coordinated chemical pathways. Most of these pathways are combinations of oxidation and reduction reactions, which occur at the same time. An oxidation reaction strips an electron from an atom in a compound, and the addition of this electron to another compound is a reduction reaction. Because oxidation and reduction usually occur together, these pairs of reactions are called redox reactions.
The removal of an electron from a molecule, results in a...
Necrosis01:16

Necrosis

Necrosis is considered as an “accidental” or unexpected form of cell death that ends in cell lysis. The first noticeable mention of “necrosis” was in 1859 when Rudolf Virchow used this term to describe advanced tissue breakdown in his compilation titled “Cell Pathology”.
Morphological Manifestations of Necrosis
Necrotic cells show different types of morphological appearance depending on the type of tissue and infection. In coagulative necrosis, cells become anucleated and die, but their...
Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox property is crucial in...
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
Radical Autoxidation01:20

Radical Autoxidation

The oxidation of an organic compound in the presence of air or oxygen is called autoxidation. For example, cumene reacts with oxygen to form hydroperoxide. Autoxidation involves initiation, propagation, and termination steps. Many organic compounds are susceptible to autoxidation—especially ethers in the presence of oxygen, which form hydroperoxides. Even though this reaction is slow, old ether bottles contain small amounts of peroxide, which leads to laboratory explosions during ether...
Hemoglobin01:24

Hemoglobin

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...