Biochemistry, Department of

 

Document Type

Article

Date of this Version

2014

Citation

THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 289, NO. 43, pp. 29836–29858, October 24, 2014

Comments

© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

Abstract

Background: Heme oxygenase, cytochrome P450 reductase, and biliverdin reductase are the key enzymes in heme degradation.

Results: Specific electrostatic and hydrophobic interactions form the binding interface between heme oxygenase and cytochrome P450 reductase. Conclusion: Heme oxygenase binds cytochrome P450 reductase dynamically and biliverdin reductase very weakly.

Significance: Characterizing interactions among proteins involved in heme degradation are crucial to understanding heme homeostasis.

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