Design of a novel P450: A functional bacterial-human cytochrome P450 chimera

Miyuki Shimoji, Hequn Yin, Lee Ann Higgins, Jeffrey P. Jones

Research output: Contribution to journalArticlepeer-review

28 Scopus citations


We report the construction of a functional chimera from approximately 50% bacterial (cytosolic) cytochrome P450cam and 50% mammalian (membrane- bound) cytochrome P450 2C9. The chimeric protein shows a reduced CO- difference spectrum absorption at 446 nm, and circular dichroism spectra indicate that the protein is globular. The protein is soluble and catalyzes the oxidation of 4-chlorotoluene using molecular oxygen and reducing equivalents from bacterial putidaredoxin and putidaredoxin reductase. This chimera provides a novel method for addressing structure-function issues and may prove useful in the design of oxidants for benign and stereospecific synthesis, as well as catalysts for bioremediation of polluted areas. Furthermore, these results provide the first evidence that bacterial P450 enzymes and mammalian P450 enzymes are likely to share a common tertiary structure.

Original languageEnglish (US)
Pages (from-to)8848-8852
Number of pages5
Issue number25
StatePublished - Jun 23 1998


Dive into the research topics of 'Design of a novel P450: A functional bacterial-human cytochrome P450 chimera'. Together they form a unique fingerprint.

Cite this