Cytochromes P450 are known to exhibit diverse catalytic functions against a large number of hydrocarbon substrates. The determinants of specific activity(ies) that operate on specific substrates have not been widely explored. Earlier, we showed that dehalogenation of 1,2-dibromo-3-chloropropane (DBCP) by P450cam (CYP101) monooxygenase exhibits oxygen- and substrate-dependent product distributions and reaction rates (1). Bromochloroacetone was the major conversion product when incubation media were saturated with oxygen, whereas allyl chloride was the sole product accounting for virtually all of the DBCP converted in the absence of oxygen. In an effort to develop a quantitative understanding of the effect of oxygen on product distribution and reaction rate, we have identified first generation products and measured reaction rates at four oxygen levels ranging from 0.01% to 100% saturation. In addition to bromochloroacetone and allyl chloride, a number of bromochloropropene isomers were identified in the presence of oxygen and are thought to be formed by an elimination mechanism. These products accounted for greater than 97 mol % of the reacted DBCP, which was run to high conversion (60-100 mol % DBCP converted). These measurements suggest that P450cam acts on the DBCP substrate through hydroxylation to produce 1-bromo-3-chloroacetone, through reduction to produce allyl chloride, and through elimination to produce bromochloropropene, with oxygen concentration determining the extent of each activity. A global data fitting kinetic model that describes the time-varying concentrations of substrate and products was developed to quantify the controlling level of oxygen on these multiple activities. The parameters of the model were compared with independent measurements and data from the literature.