School of Humanities and Sciences
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Edward I. Solomon
Monroe E. Spaght Professor of Chemistry and Professor of Photon Science
Current Research and Scholarly InterestsProf. Solomon's work spans physical-inorganic, bioinorganic, and theoretical-inorganic chemistry, focusing on spectroscopic elucidation of the electronic structure of transition metal complexes and its contribution to reactivity. He has advanced our understanding of metal sites involved in electron transfer, copper sites involved in O2 binding, activation and reduction to water, structure/function correlations over non-heme iron enzymes, and correlation of biological to heterogeneous catalysis.
David and Lucile Packard Professor in Marine Science, Emeritus
Current Research and Scholarly InterestsWe examine two aspects of organism-environment interactions: How does stress from physical (e.g., temperature) and chemical (oxygen levels, pH) factors perturb organisms and how do organisms respond, adaptively, to cope with this stress? We examine evolutionary adaptation and phenotypic acclimatization using a wide variety of marine animals, including Antarctic fishes and invertebrates from intertidal habitats on the coastlines of temperate and tropical seas.
Professor of Chemical Engineering, of Materials Science and Engineering and, by courtesy, of Applied Physics
Current Research and Scholarly InterestsTheory and computation of biological processes and complex materials
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.
Surface Immobilization of Catalysts in Mesoporous Materials
In redox active biological metal sites, the ligation environment is coupled tightly to the functional chemistry. Yet, the metal sites are also site-isolated, creating species that may only have a transient existence in a homogeneous solution. Site isolation of synthetic complexes can be achieved synthetically by supporting the metal complex on a solid matrix. Movement of these complexes into silica based materials or onto electroactive carbon electrodes represent a new direction for the group in the development of bio-inspired metal-based catalysts.
Acting Dean of Research, Frank Lee and Carol Hall Professor, Senior Associate Vice Provost of Research and Professor of Genetics
Current Research and Scholarly InterestsWe use the tools of genetics, microscopy, and biochemistry to understand fundamental questions of cell biology: How are cells organized by the cytoskeleton? How do the centrosome and cilium control cell control cell signaling? How is cell division coordinated with duplication of the centrosome, and what goes wrong in cancer cells defective in this coordination?