Stanford University
Showing 101-120 of 301 Results
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Keith Hodgson
David Mulvane Ehrsam and Edward Curtis Franklin Professor of Chemistry and Professor of Photon Science
BioCombining inorganic, biophysical and structural chemistry, Professor Keith Hodgson investigates how structure at molecular and macromolecular levels relates to function. Studies in the Hodgson lab have pioneered the use of synchrotron x-radiation to probe the electronic and structural environment of biomolecules. Recent efforts focus on the applications of x-ray diffraction, scattering and absorption spectroscopy to examine metalloproteins that are important in Earth’s biosphere, such as those that convert nitrogen to ammonia or methane to methanol.
Keith O. Hodgson was born in Virginia in 1947. He studied chemistry at the University of Virginia (B.S. 1969) and University of California, Berkeley (Ph.D. 1972), with a postdoctoral year at the ETH in Zurich. He joined the Stanford Chemistry Department faculty in 1973, starting up a program of fundamental research into the use of x-rays to study chemical and biological structure that made use of the unique capabilities of the Stanford Synchrotron Radiation Lightsource (SSRL). His lab carried out pioneering x-ray absorption and x-ray crystallographic studies of proteins, laying the foundation for a new field now in broad use worldwide. In the early eighties, he began development of one of the world's first synchrotron-based structural molecular biology research and user programs, centered at SSRL. He served as SSRL Director from 1998 to 2005, and SLAC National Accelerator Laboratory (SLAC) Deputy Director (2005-2007) and Associate Laboratory Director for Photon Science (2007-2011).
Today the Hodgson research group investigates how molecular structure at different organizational levels relates to biological and chemical function, using a variety of x-ray absorption, diffraction and scattering techniques. Typical of these molecular structural studies are investigations of metal ions as active sites of biomolecules. His research group develops and utilizes techniques such as x-ray absorption and emission spectroscopy (XAS and XES) to study the electronic and metrical details of a given metal ion in the biomolecule under a variety of natural conditions.
A major area of focus over many years, the active site of the enzyme nitrogenase is responsible for conversion of atmospheric di-nitrogen to ammonia. Using XAS studies at the S, Fe and Mo edge, the Hodgson group has worked to understand the electronic structure as a function of redox in this cluster. They have developed new methods to study long distances in the cluster within and outside the protein. Studies are ongoing to learn how this cluster functions during catalysis and interacts with substrates and inhibitors. Other components of the protein are also under active study.
Additional projects include the study of iron in dioxygen activation and oxidation within the binuclear iron-containing enzyme methane monooxygenase and in cytochrome oxidase. Lab members are also investigating the role of copper in electron transport and in dioxygen activation. Other studies include the electronic structure of iron-sulfur clusters in models and enzymes.
The research group is also focusing on using the next generation of x-ray light sources, the free electron laser. Such a light source, called the LCLS, is also located at SLAC. They are also developing new approaches using x-ray free electron laser radiation to image noncrystalline biomolecules and study chemical reactivity on ultrafast time scales. -
Wray Huestis
Professor of Chemistry, Emerita
BioProfessor Wray Huestis’ research concerns the molecular mechanisms whereby cells control their shape, motility, deformability and the structural integrity of their membranes. Metabolic control of interprotein and protein-lipid interactions is studied by a variety of biochemical, spectroscopic and radiochemical techniques, including fluorescence and EPR spectrometry, autoradiography and electron microscopy. The role of lipid metabolism and transport in regulating the fluid dynamics of cell suspensions (red blood cells, platelets, lymphocytes) is examined using circulating cells and cells grown in culture. Cell-cell and cell-liposome interactions are studied using model membrane systems with widely differing physical properties. Complexes of liposomes and encapsulated viruses are used as selective vectors to deliver water-soluble compounds across the membranes of intact cells. The particular projects described in the listed publications have as a common goal an understanding of the molecular workings of the cell membrane.
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Matthew Kanan
Professor of Chemistry and Senior Fellow at the Precourt Institute for Energy
BioMatt Kanan is a Professor of Chemistry and Senior Fellow at the Precourt Institute for Energy at Stanford. Matt’s research group works across multiple fields of chemistry and engineering with applications for sustainable plastics, critical mineral recovery, and carbon management. Their work has led to several inventions in these areas, including new performance-advantaged bioplastics, electrochemical systems to recycle acid and base, metal-free catalysts for C1 transformations, and thermal mineral conversion processes. Matt is the co-founder of ReSource Chemical Corp., an Oakland-based start-up commercializing manufacturing technology developed in his lab, and Mafix, Inc., a spin-out developing mineral fertilizers that remove CO2 from the atmosphere. Prior to joining the Stanford faculty in 2009, Matt did his Ph.D. studies in organic chemistry at Harvard and postdoctoral research at MIT in inorganic chemistry. He earned his B.A. in chemistry from Rice University in 2000.
