The figure shows the crystal structure of a form of cytochrome P450 (CYP), CYP1A2, a form closely related to CYP1B1, an uncrystallized form of Family 1 CYP, with which it has been aligned to reveal structural impact of mutations.1 Choudhary D, Jansson I, Sarfarazi M, Schenkman JB: Characterization of the biochemical and structural phenotypes of four CYP1B1 mutations observed in individuals with primary congenital glaucoma. Pharmacogenet Genomics 2008;18:665-676. The yellowed residue labelled Cys is cysteine, which forms the 5th heme ligand of the heme, and other yellow residues represent some of the mutation sites in CYP1B1causing primary congenital glaucoma. White letters on the cylinders indicate a-helices of CYP1A2.2Sansen S, Yano JK, Reynald RL, Schoch GA, Griffin KJ, Stout CD, Johnson EF: Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. Journal of Biological Chemistry 2007;282:14348-14355.
Research in our laboratory revolves around the hemoprotein enzymes cytochrome P450, an enzyme superfamily that we have studied for more than three decades. Our studies have involved the chemistry, biochemistry, enzymology and developmental roles of this cellular membrane protein, and its interaction with other cellular proteins.
John B. Schenkman Lab
UConn Health Center
263 Farmington Avenue
Farmington, CT 06030-3505
