Structural Studies on Prokaryotic Cytochromes P450

The camphor monooxygenase from Pseudomonas putida, P450cam, has been the single best paradigm for P450 structure and function studies for over two decades.1 Following a wealth of biochemical and biophysical studies on P450cam, the high-resolution crystal structure became available in 1987.2 This was followed by a series of structures on various inhibitor/substrate complexes which revealed some key structure-function relationships in P450s. In addition, with the development of recombinant expression systems for P450cam, it has been possible to use site-directed mutagenesis3,4 with reference to the crystal structure to probe questions of how structure relates to function.

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