A model of the membrane-bound cytochrome b5-cytochrome P450 complex from NMR and mutagenesis data

Shivani Ahuja, Nicole Jahr, Sang Choul Im, Subramanian Vivekanandan, Nataliya Popovych, Stéphanie V. Le Clair, Rui Huang, Ronald Soong, Jiadi Xu, Kazutoshi Yamamoto, Ravi P. Nanga, Angela Bridges, Lucy Waskell, Ayyalusamy Ramamoorthy

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Abstract

Background: cytb5 modulates catalysis performed by cytsP450, in vivo and in vitro. Results: The structure of full-length cytb5 was solved by NMR, and the cytP450-binding site on cytb5 was identified by mutagenesis and NMR. Conclusion: A model of the cytb5-cytP450 complex is presented. Addition of a substrate strengthens the cytb 5-cytP450 interaction. Significance: The cytb5-cytP450 complex structure will help unravel the mechanism by which cytb5 regulates catalysis by cytP450.

Original languageEnglish (US)
Pages (from-to)22080-22095
Number of pages16
JournalJournal of Biological Chemistry
Volume288
Issue number30
DOIs
Publication statusPublished - Jul 26 2013

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All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Ahuja, S., Jahr, N., Im, S. C., Vivekanandan, S., Popovych, N., Le Clair, S. V., ... Ramamoorthy, A. (2013). A model of the membrane-bound cytochrome b5-cytochrome P450 complex from NMR and mutagenesis data. Journal of Biological Chemistry, 288(30), 22080-22095. https://doi.org/10.1074/jbc.M112.448225