Related Experiment Video
Updated: Aug 13, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
Iron release from metmyoglobin, methaemoglobin and cytochrome c by a system generating hydrogen peroxide
1Agricultural Research Organization, Volcani Center, Department of Food Science, Bet-Dagan, Israel.
Abstract:
The reaction of H2O2 with resting metmyoglobin (MetMb), methaemoglobin (MetHb) and cytochrome-c (Cyt-c) was studied in the Soret and visible regions. The differences between the original and the final peak heights of the native haemproteins at 408 nm was found to be directly proportional to the loss of iron from the molecule. The release of iron from haemproteins was studied in a system generating H2O2 continuously at a low rate by an enzymic system, or by addition of large amounts of H2O2. Cytochrome-c, methaemoglobin and metmyoglobin during interaction with H2O2 at a concentration of 200 microM release 40%, 20% and 3%, respectively, of molecular iron after 10 min. The inhibition of haem degradation and iron release by enzymatically-generated H2O2 was determined using several hydroxyl radical scavengers, reducing agents and antioxienzymes, such as superoxide dismutase, catalase and caeruloplasmin.
More Related Videos
Related Concept Videos
The Electron Transport Chain
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q in...
Peroxisomes
Oxidation of Phenols to Quinones
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 IV
Bioactivation and Tissue Toxicity
Metabolism of Chemolithotrophs
![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
