SLAC National Accelerator Laboratory
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Professor of Photon Science
BioHedman’s research program is focused on the development and applications of x-ray absorption and emission spectroscopies using synchrotron radiation, with a scientific emphasis primarily on study of the electronic and structural aspects of metal ion active sites in bioinorganic and biological systems. A common theme is to investigate how structure at molecular and macromolecular levels relates to function.
A major long-term focus has been the active site of the enzyme nitrogenase, and the various nitrogenase metal clusters, including elucidating the electronic and geometric structure of those that are formed and changed along their biosynthetic pathways. Other systems of systematic studies include iron-sulfur cluster containing enzymes, blue and multi-copper proteins, heme-copper oxidases, and iron-containing oxidases. Methods developments include x-ray absorption spectroscopy (edge and extended fine structure - or EXAFS), including the application of multiple-scattering analysis in EXAFS studies of metal clusters relevant to bioinorganic systems, the development of methodology for polarized single crystal x-ray absorption spectroscopy, and methodology and instrumentation development for soft- through hard-energy XAS.
Hedman received her B.S and B.A. in Chemistry, M.Sc. in Inorganic Chemistry, and Ph.D. in Chemistry from the University of Umeå, Sweden. She was Assistant Professor (equivalent) in Inorganic Chemistry at the University of Umeå before coming to Stanford, initially as Senior Academic Scientific Staff, followed by appointed as Professor (Research) in 2002, and Professor of Photon Science in 2007.
Professor of Applied Physics and of Photon Science and, by courtesy, of Electrical Engineering
Current Research and Scholarly InterestsElectronic properties and dynamics of nanoscale materials, ultrafast lasers and spectroscopy.
David Mulvane Ehrsam and Edward Curtis Franklin Professor of Chemistry and Professor of Photon Science at SLAC
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.