Cytochrome P450 enzymes are hemoproteins found in all organisms, and responsible for the oxidation of many endogenous substances and xenobiotics as part of normal metabolism and detoxification processes. The P450-catalyzed monooxygenation reactions can however lead to the activation of certain environmental procarcinogens, particularly polyaromatic hydrocarbons (PAHs). In an attempt to understand the mechanisms of action of these enzymes, inhibitors have been developed to probe into their active site pockets. O-alkylresorufins fluoresce when dealkylated by P450 enzymes. By measuring the florescence intensity of the resorufin anion formed during the dealkylation reaction, enzyme activity and its inhibition by various inhibitors can be monitored. Our group has designed and synthesized a novel set of resorufin derivatives that have the potential to be used as inhibitor indicators in inhibition studies.

Synthesis of resorufin derivatives as inhibitor indicators of cytochrome P450 enzymes

247th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.