Heme is a porphyrin that is the important non-protein component of hemoglobin.
The general pathway for heme and chlorophyll biosynthesis has been well known yet several of the enzymes are as yet poorly understood in terms of active site amino acids and catalytic mechanisms. In this lab, we study two of the enzymes involved in heme biosynthesis and are especially interested in the molecular recognition of substrate by the enzymes. Synthetic substrate analogs are used to probe the substrate fit into the active site of the two specific enzymes, Coproporphyrinogen Oxidase and Uroporphyrinogen Decarboxylase. Enzymic activities are evaluated following extractions and HPLC evaluation. Covalent modification of active site amino acids is also an important method being used to evaluate enzyme activity of both crude and partially purified proteins.