Chemistry Student Seminar: Saurabh Ahirwar

Abstract

Exploring the activity and the selectivity of monooxygenase enzymes from Novosphingobium aromaticivorans.

Cytochrome P450 enzymes (P450s) were discovered in 1958 by Garfinkel and Klingenberg. These enzymes make up a superfamily of haem monooxygenase which catalyse a diverse range of biological oxidative transformations. P450s, which catalyse the insertion of an oxygen atom from atmospheric dioxygen into a carbon-hydrogen bond, are found across all kingdoms of life.

In prokaryotic organisms they are involved in a number of important biosynthetic oxidation reactions. Due to the characteristics of these enzymes, they have been widely studied for the synthesis of fine chemicals and intermediates which are very difficult to synthesize using conventional chemical techniques.

CYP101B1 and CYP101C1 are P450 enzymes from the bacterium Novosphingobium aromaticivorans DSM12444. Both use a common electron transfer system, consisting of a ferredoxin reductase and a ferredoxin and are capable of acting on substrates including terpenes and norisoprenoids.

This project attempts to address the oxidation behaviour and further explore the substrate range and catalytic potential for both the enzymes.