Karine Auclair grew up in Jonquière, Québec. She completed a Honor's B.Sc. in Chemistry at the Université du Québec à Chicoutimi in 1994. She then undertook a Ph.D. with Professor John C. Vederas (as an NSERC 1967 Awardee) in organic chemistry at the University of Alberta. In the course of her graduate studies, Karine Auclair contributed to dramatically improve our understanding of the biosynthesis of the cholesterol-lowering agent lovastatin by fungi. She was also the first to purify a natural Diels-Alderase, lovastatin nonaketide synthase (LNKS or LovB). Her work involved synthesis, natural product structure elucidation, biosynthetic incorporation experiments, cell free extract preparation, and protein purification. She also prepared a series of tethered triene that were tested as Diels-Alder substrates in the presence of commercially available enzymes or LNKS.
After she graduated in 1999, she joined the research group of Professor Ortiz de Montellano at the University of California (San Francisco) for a post-doctoral research position. For the following two years, her work involved studies of two families of heme proteins using techniques as varied as cloning, mutagenesis, and spectroscopy. The mechanism of P450 enzymes were studied using three different tools: 1) Mutation of the proximal thiolate heme iron ligand which led to the discovery of new roles for this ligand; 2) Radical clocks to demonstrate the formation of a radical intermediate and a measure of its lifetime (collaboration with Prof. Groves, Princeton University); 3) Photoaffinity labeling probes to study the geometry of the enzyme active site. The second group of enzymes studied was the heme oxygenases (HOs). In collaboration with Prof. LaMar, University of California, Davis, she participated in the elucidation of the human HO-1 structures by NMR. She also prepared fusion proteins of human HO-1 with P450 reductase and with glutathione-S-transferase.