Valine residues cytochrome

Models have been developed to accommodate the results of the hydroxyla-tion of substrates with different structures. The cytochrome P450CAM camphor hydroxylase from the bacterium Pseudomonas putida has been studied by X-ray crystallography. The importance of hydrophilic interactions with a valine (VAL-247) and a polar interaction mediated by hydrogen bonding to a tyrosine residue (TYR-96) has been noted. A model based on the hydroxylation of numerous cyclic amides by Beauveria sulfurescens (originally named Sporotrichum sulfurescens) showed that hydroxylation occurred preferentially at a methylene group about 5.5 A from an electron-rich substituent on the substrate. 

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