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Tetrapyrroles pp 101–115Cite as

Heme Degradation:

Mechanistic and Physiological Implications

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Part of the book series: Molecular Biology Intelligence Unit ((MBIU))

Abstract

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.

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Authors and Affiliations

  1. Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, 20 Penn Street, Baltimore, Maryland, 21201, USA

    Angela Wilks

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  1. Angela Wilks
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Correspondence to Angela Wilks .

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© 2009 Landes Bioscience and Springer Science+Business Media

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Wilks, A. (2009). Heme Degradation:. In: Tetrapyrroles. Molecular Biology Intelligence Unit. Springer, New York, NY. https://doi.org/10.1007/978-0-387-78518-9_6

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