Keith Hodgson
Title: The Howard H. and Jessie T. Watkins University Professor of Chemistry and the Stanford Synchrotron Radiation Lightsource
Education: B.S., 1969, University of Virginia; Ph.D., 1972, University of California at Berkeley
Professional Academic History: Postdoctoral, Eidgenössische Technische Hochschule, Zürich, Switzerland, 1973. Assistant Professor, Chemistry, Stanford, 1973-1979. Associate Professor, Chemistry, Stanford, 1979-1984. Professor, Chemistry, Stanford, 1984-present. Assistant Director, SSRL, 1980-1995. Deputy Director, SSRL, 1996-1997. Director, SSRL, 1997-2005. SLAC Photon Science Director, 2005 - present. Howard H. and Jessie T. Watkins Stanford University Professor of Chemistry and Photon Science, 2002-present.
Awards: NATO Postdoctoral Fellow, E.T.H. (Zurich) 1972-73, Alfred P. Sloan Foundation Fellow, 1976-78; Sidhu Award for Contributions to X-ray Diffraction, 1978; World Bank Lecturer, 1984, E.O. Lawrence Award, 2002
Principal Research Interests: Inorganic, Bioinorganic, Structural and Biophysical Chemistry with a focus on the fields of bioinorganic and biophysical chemistry. In general, his research involves asking how structure at different organizational levels relates to function. Studies are being done at the molecular and macromolecular levels using a number of x-ray spectroscopic and scattering techniques such as x-ray absorption spectroscopy (XAS) on a variety of different scientific problems.
Of particular interest is the active site of the enzyme nitrogenase, responsible for conversion of atmospheric dinitrogen to ammonia. Current studies have revealed that the molybdenum is contained in a polynuclear Mo-Fe-S cluster. From XAS studies at S, Fe and Mo, his group has studied the electronic distribution as a function of redox in this cluster and has recently developed new methods to study long distances in the cluster within and outside the protein. Studies are now 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.
Other projects include the study of iron in dioxygen activation and oxidation (in the binuclear iron-containing enzyme methane monooxygenase and in cytochrome oxidase), and the role of copper in electron transport and in dioxygen activation.