School of Humanities and Sciences
Showing 11-20 of 22 Results
Associate Professor of Chemistry, Emeritus
Current Research and Scholarly InterestsThe Chidsey group research interest is to build the chemical base for molecular electronics. To accomplish this, we synthesize the molecular and nanoscopic systems, build the analytical tools and develop the theoretical understanding with which to study electron transfer between electrodes and among redox species through insulating molecular bridges
William R. Kenan Jr. Professor, Professor of Molecular and Cellular Physiology and of Energy Science and Engineering
Current Research and Scholarly InterestsSynthesis, functionalization and applications of nanoparticle bioprobes for molecular cellular in vivo imaging in biology and biomedicine. Linear and nonlinear difference frequency mixing ultrasound imaging. Lithium metal-sulfur batteries, new approaches to electrochemical splitting of water. CO2 reduction, lithium extraction from salt water
Vice Provost for Undergraduate Education, Freeman-Thornton Chair for the Vice Provost for Undergraduate Education and Professor of Physics
Current Research and Scholarly InterestsExperimental & Observational Astrophysics and Cosmology
George A. and Hilda M. Daubert Professor of Chemistry, Emeritus
BioProfessor Emeritus James Collman has made landmark contributions to inorganic chemistry, metal ion biochemistry, homogeneous catalysis, and transition metal organometallic chemistry. He pioneered numerous now-popular research tools to reveal key structural and functional details of metalloenzymes essential to respiration and energy, and hemoglobin and myoglobin, essential to oxygen transport in the blood.
Born 1932 in Beatrice, Nebraska, James P. Collman studied chemistry at U. Nebraska–Lincoln (B.S. 1954, M.S. 1956). His doctoral work at U. Illinois at Urbana-Champaign (Ph.D., 1958) focused on Grignard reagents. As a faculty member at U. North Carolina, he demonstrated aromatic reactivity in metal acetylacetonates, and he developed metal complexes that hydrolyze peptide bonds under physiological conditions. He came to Stanford University as Professor of Chemistry in 1967. Among many honors, Prof. Collman’s was elected to the National academy of Sciences in 1975, and named California Scientist of the Year in 1983.
At Stanford, Prof. Collman invented a new paradigm for studying biological systems using functional synthetic analogs of metal-containing enzyme systems, free from the protein coatings that can affect metalloprotein chemical properties. This strategy allowed him to elucidate the intrinsic reactivity of the metal center as well as the effects of protein-metal interactions on biological function.
One focal point of this research has involved heme-proteins such as the oxygen (O2) carrier hemoglobin (Hb), and the O2-storing protein myoglobin (Mb). Prof. Collman was the first to prepare and characterize stable, functional analogues of the Hb and Mb active sites, which contain an iron derivative of the large flat “porphyrin” ligand. In his “picket fence” porphyrin, groups installed on the periphery block side reactions, which would otherwise degrade the structure. This protected iron complex manifests the unique magnetic, spectroscopic and structural characteristics of the O2-binding Hb and Mb sites, and exhibits very similar O2-binding affinities.
The Collman Group also prepared functional mimics of the O2-binding/reducing site in a key respiration enzyme, cytochrome c oxidase, CcO, which converts O2 to H2O during biosynthesis of the energy storage molecule ATP. This enzyme must be very selective: partial O2 reduction products are toxic. Prof. Collman invented a powerful synthetic strategy to create analogs of the CcO active site and applied novel electrochemical techniques to demonstrate that these models catalyze the reduction of O2 to water without producing toxic partially-reduced species. He was able to mimic slow, rate-limiting electron delivery by attaching his CcO model to a liquid-crystalline membrane using “click chemistry.” He demonstrated that hydrogen sulfide molecules and heterocycles reversibly bind to the metal centers at CcO’s active site, connecting a synthetic enzyme model to simple molecules that reversibly inhibit respiration. These respiration inhibitors exhibit physiological properties, affecting blood clotting and controlling the effects of the hormone, nitric oxide, NO.
In addition, Prof. Collman performed fundamental studies of organometallic reactions. He also prepared and characterized homodinuclear and heterodinuclear complexes having metal-metal multiple bonds, and made the first measurements of the rotational barriers found in multiple metal-metal bonds.
Prof. Collman’s impactful textbook “Principles and Applications of Organotransition Metal Chemistry” has seen multiple editions. His book “Naturally Dangerous: Surprising Facts About Food, Health, and the Environment” explains the science behind everyday life, and received favorable reviews in Nature and The Washington Post.
Assistant Professor of Biology
Current Research and Scholarly InterestsWe are a highly interdisciplinary research team, joined in our desire to better understand microbial life. To elucidate how bacterial cells accumulate biomass and grow, we work with the model organism Escherichia coli. We further focus on gut bacteria and their interactions with the human host. Our approaches combine quantitative experimentation and mathematical modeling.
Edward Ricketts Provostial Professor, Professor of Oceans, Senior Fellow at the Woods Institute for the Environment and Professor, by courtesy, of Biology
Current Research and Scholarly InterestsEcology, conservation, fisheries, protected species, ecosystem-based management
Job and Gertrud Tamaki Professor of Chemistry
Current Research and Scholarly InterestsOur objective is to develop new biophysical methods to advance current understandings of cellular machinery in the complicated environment of living cells. Currently, we are focusing on four research areas: (1) Membrane curvature at the nano-bio interface; (2) Nanoelectrode arrays (NEAs) for scalable intracellular electrophysiology; (3) Electrochromic optical recording (ECORE) for neuroscience; and (4) Optical control of neurotrophin receptor tyrosine kinases.