Stanford University
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Daniel Stack
Associate Professor of Chemistry
BioResearch in the Stack group focuses on the mechanism of dioxygen activation and the subsequent oxidative reactivity with primarily copper complexes ligated by imidazoles or histamines. Specifically, the group is interested in substrate hydroxylations and full dioxygen reduction. The remarkable specificity and energy efficiency of metalloenzymes provide the inspiration for the work. Trapping and characterizing immediate species, primarily at low temperatures, provide key mechanistic insights especially through substrate reactivity along with spectroscopic and metrical correlation to DFT calculations. Our objective is to move these efficient enzymatic mechanisms into small synthetic complexes, not only to reproduce biological reactivity, but more importantly to move the oxidative mechanism beyond that possible in the protein matrix.
Daniel Stack was born, raised and attended college in Portland Oregon. He received his B.A. from Reed College in 1982 (Phi Beta Kappa), working with Professor Tom Dunne on weak nickel-pyrazine complexes. In Boston, he pursued his doctoral study in synthetic inorganic chemistry at Harvard University (Ph.D., 1988) with Professor R. H. Holm, investigating site-differentiated synthetic analogues of biological Fe4S4 cubanes. As an NSF Postdoctoral Fellow with Professor K. N. Raymond at the University of California at Berkeley, he worked on synthesizing new, higher iron affinity ligands similar to enterobactin, a bacterial iron sequestering agent. He started his independent career in 1991 at Stanford University primarily working on oxidation catalysis and dioxygen activation, and was promoted to an Associate Professor in 1998. His contributions to undergraduate education have been recognized at the University level on several occasions, including the Dinkelspiel Award for Outstanding Contribution to Undergraduate Education in 2003.
Areas of current focus include:
Copper Dioxygen Chemistry
Our current interests focus on stabilizing species formed in the reaction of dioxygen with Cu(I) complexes formed with biologically relevant imidazole or histamine ligation. Many multi-copper enzymes ligated in this manner are capable of impressive hydroxylation reactions, including oxidative depolymerization of cellulose, methane oxidation, and energy-efficient reduction of dioxygen to water. Oxygenation of such complexes at extreme solution temperatures (-125°C) yield transient Cu(III) containing complexes. As Cu(III) is currently uncharacterized in any biological enzyme, developing connections between the synthetic and biological realms is a major focus.
