Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's

Kurumbail G. Ravichandran, Sekhar S. Boddupalli, Charles A. Hasemann, Julian A. Peterson, Johann Deisenhofer

Research output: Contribution to journalArticlepeer-review

914 Scopus citations


Cytochrome P450BM-3, a bacterial fatty acid monooxygenase, resembles the eukaryotic microsomal P450's and their flavoprotein reductase in primary structure and function. The three-dimensional structure of the hemoprotein domain of P450BM-3 was determined by x-ray diffraction and refined to an R factor of 16.9 percent at 2.0 angstrom resolution. The structure consists of an α and β domain. The active site heme is accessible through a long hydrophobic channel formed primarily by the âdomain and the B′ and F helices of the ádomain. The two molecules in the asymmetric unit differ in conformation around the substrate binding pocket. Substantial differences between P450BM-3 and P450cam, the only other P450 structure available, are observed around the substrate binding pocket and the regions important for redox partner binding. A general mechanism for proton transfer in P450's is also proposed.

Original languageEnglish (US)
Pages (from-to)731-736
Number of pages6
Issue number5122
StatePublished - 1993

ASJC Scopus subject areas

  • General


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