Tetrapyrroles pp 101-115 | Cite as

Heme Degradation:

Mechanistic and Physiological Implications
  • Angela Wilks
Part of the Molecular Biology Intelligence Unit book series (MBIU)


Heme oxidation catalyzed by heme oxygenase has evolved to carry out a number of important and diverse physiological processes including iron reutilization and cellular signaling in mammals, synthesis of light-harvesting pigments in cyanobacteria, light perception in plants, and the acquisition of iron in bacterial pathogens. In mammals the evolution of biliverdin IXα reductase in the conversion of biliverdin IXα to bilirubin IXα provides an important link between heme metabolism and antioxidant protection. The following review will address heme degradation in the context of the physiological and mechanistic aspects of heme oxidation and biliverdin reduction in animals and bacteria, and the possible clinical ramifications of modulation of heme oxygenase and biliverdin reductase activity.


Cytochrome P450 Reductase Heme Degradation Flavin Reductase Heme Metabolism Biliverdin Reductase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Landes Bioscience and Springer Science+Business Media 2009

Authors and Affiliations

  1. 1.Department of Pharmaceutical Sciences, School of PharmacyUniversity of MarylandBaltimoreUSA

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