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The products, stoichiometry, and kinetics of the oxidation of the enzyme cytochrome P-450 cam by five polyhalomethanes and chloronitromethane are described. The reactivity of the enzyme is compared with that of deuteroheme and with the enzyme in its native cell, Pseudomonas putida (PpG-786). In all cases, the reaction entails hydrogenolysis of the carbon-halogen bond: 2FeIIP + RCXn----2FeIIIP + RCHXn-1 (P = porphyrin or P-450 cam in vitro and in vivo). Trichloronitromethane was the fastest reacting substrate, and chloroform was the slowest. The results establish that P. putida is a valid whole cell model for the reductase activity of the P-450 complement in these reactions. The reactions of cytochrome P-450 with polyhaloalkanes proceed in a manner quite analogous to other iron(II) proteins in the G conformation. The chemistry observed for the enzyme parallels that of its iron(II) porphyrin active site. Iron-bonded carbenes are not intermediates, and hydrolytically stable iron alkyls are not products of these reactions.

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