A critical role of protein‐bound water in the catalytic cycle of cytochrome P‐450 camphor

Abstract
The rates of NADH oxidation during the hydroxylation of camphor by cytochrome P‐450cam were followed in the presence of co‐solvents used to increase the osmotic pressure surrounding the protein‐bound water. As a result, the measured V max decreases independently of the perturbant tested. Roughly 28 molecules of water, involved during the catalytic cycle, are deduced from the variation of V max as a function of osmotic pressure. These molecules, in part, could be those present in the cytochrome P.450cam‐putidaredoxin interface.