School of Humanities and Sciences


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  • James Collman

    James Collman

    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.

  • Vinícius Wilian D. Cruzeiro

    Vinícius Wilian D. Cruzeiro

    Postdoctoral Scholar, Chemistry

    BioVinícius Cruzeiro explores computational/theoretical chemistry aiming at accurately describing the behavior of proteins, biomolecules, and related systems using molecular simulations, quantum mechanics, and machine learning representations. This research digs into fundamental aspects of nature at the intersection of physics, chemistry, and biology. The knowledge gained is employed to complement experiments (that cannot achieve atomic detail) and can drive the design of new materials and pharmaceutical applications, such as in drug discovery. Dr. Cruzeiro actively collaborates with experimentalists and other theoretical researchers.

    Dr. Cruzeiro is part of the Amber developer’s team. He has participated in developing different methodologies, including molecular simulations with coupled electrochemical and pH effects, enhanced sampling techniques, and quantum mechanics/molecular mechanics approaches. Amber is a popular software package for molecular simulations used by several research groups worldwide.

  • Bianxiao Cui

    Bianxiao Cui

    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.

  • Yi Cui

    Yi Cui

    Director, Precourt Institute for Energy, Fortinet Founders Professor, Professor of Materials Science and Engineering, of Photon Science, Senior Fellow at the Woods Institute for the Environment and Professor, by courtesy, of Chemistry

    BioCui studies fundamentals and applications of nanomaterials and develops tools for their understanding. Research Interests: nanotechnology, batteries, electrocatalysis, wearables, 2D materials, environmental technology (water, air, soil), cryogenic electron microscopy.