Protein/Protein Interactions in the Mammalian Heme Degradation Pathway HEME OXYGENASE-2, CYTOCHROME P450 REDUCTASE, AND BILIVERDIN REDUCTASE

Authors

• Andrea L. M. Spencer, University of Michigan, Ann Arbor
• Ireena Bagai, University of Michigan, Ann ArborFollow
• Donald F. Becker, University of Nebraska-LincolnFollow
• Erik R. P. Zuiderweg, University of Michigan, Ann ArborFollow
• Stephen W. Ragsdale, University of Michigan, Ann ArborFollow

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.