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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The formation of the 7-carboxyheptyl radical from 13-hydroperoxy-9,11-octadecadienoic acid catalyzed by hemoglobin and myoglobin under anaerobic conditions.

Methemoglobin (MetHb), oxyhemoglobin (oxyHb), metmyoglobin (metMb), and oxymyoglobin (oxyMb) catalyze formation of the 7-carboxyheptyl and pentyl radicals from 13-hydroperoxy-9,11-octadecadienoic acid. The relative HPLC-ESR peak height of the pentyl radical to the 7-carboxyheptyl radical was found to depend on the oxygen concentration in the reaction mixture. Under aerobic conditions, the 7-carboxyheptyl radical was predominant for the reaction mixture with ferrous ions (or cytochrome c, metHb, or metMb). On the other hand, under anaerobic conditions, the pentyl radical was predominant for the reaction mixture with ferrous ions (or cytochrome c), but the 7-carboxyheptyl radical was still predominant for the reaction mixture with metHb (or metMb), suggesting that metHb (or metMb) catalyzes the reaction through a mechanism different from that in the case of ferrous ions (or cytochrome c). In order to explain the above results, a mechanism, in which molecular oxygen is not involved, is proposed for the formation of the 7-carboxyheptyl radical in the reaction mixture of 13-HPODE with metHb (or metMb) under anaerobic conditions.[1]

References

  1. The formation of the 7-carboxyheptyl radical from 13-hydroperoxy-9,11-octadecadienoic acid catalyzed by hemoglobin and myoglobin under anaerobic conditions. Iwahashi, H., Kumamoto, K., Hirai, T. J. Biochem. (2003) [Pubmed]
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