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New insights into the structure and reactivity of FeMoco using x-ray absorption and scattering techniques
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Abstracts
Bl51 NEW INSIGHTS INTO THE STRUCTURE AND REACTIVITY OF FeMoco USING X-RAY ABSORPTION AND SCATTERING TECHNIQUES Lingling Chen,a David Eliezer,b Isaac Liu,’ Hirotsugu Ts~ruta,~ Narasaiah Gavini,d William E. Newton,e Barbara K. Burgess,d Patrick Frank,’ Britt Hedmarf and Keith 0. Hodgsonayc aDepartment of Chemistry, Stanford University, Stanford, CA 94305 bDepartment of Applied Physics, Stanford University, Stanford, CA 94305 ‘Stanford Synchrotron Radiation Laboratory, Stanford University, SLAC, M.S. 69, P.O. Box 4349, Stanford, CA 94309 dDepartment of Molecular Biology and Biochemistry, University of California at Irvine, Irvine, CA 92717 eDepartment of Biochemistry and Nutrition, Virginia Polytechnical Institute, Blacksburg, VA 24061
Recent experimental results have provided new insights into the solution structure of FeMoco and how it compares with the cluster in the active MoFe-protein. X-ray absorption edge and EXAFS experiments have been carried out at the S, Fe, and MO edges of FeMoco as well as for a number of relevant inorganic cluster complexes. Analysis of EXAFS data has utilized a new approach based on theroetical parameters and multiple scattering analysis (called GNXAS) to provide more reliable information about longer-range interaction in the polynuclear FeMo cluster. Additonal information has been determined about electronic structural changes upon redox chemistry and the binding of exogeneous ligands. X-ray scattering @AS) measurments can be used to investigate the size and shape of molecules in solution. Such XAS studies have been used to probe the structure of FeMoco in solution and how it is altered by redox and ligand-binding. Taken together, these results help provide information on the structural and functional role of the various sub-cluster components of FeMoco. This work is supported by grants from NM and NSF. The x-ray absorption and scattering data were measured at the Stanford Synchrotron Radiation Laboratory which is supported by the U.S. Department of Energy and the NIH.
Abstracts
Bl51 NEW INSIGHTS INTO THE STRUCTURE AND REACTIVITY OF FeMoco USING X-RAY ABSORPTION AND SCATTERING TECHNIQUES Lingling Chen,a David Eliezer,b Isaac Liu,’ Hirotsugu Ts~ruta,~ Narasaiah Gavini,d William E. Newton,e Barbara K. Burgess,d Patrick Frank,’ Britt Hedmarf and Keith 0. Hodgsonayc aDepartment of Chemistry, Stanford University, Stanford, CA 94305 bDepartment of Applied Physics, Stanford University, Stanford, CA 94305 ‘Stanford Synchrotron Radiation Laboratory, Stanford University, SLAC, M.S. 69, P.O. Box 4349, Stanford, CA 94309 dDepartment of Molecular Biology and Biochemistry, University of California at Irvine, Irvine, CA 92717 eDepartment of Biochemistry and Nutrition, Virginia Polytechnical Institute, Blacksburg, VA 24061
Recent experimental results have provided new insights into the solution structure of FeMoco and how it compares with the cluster in the active MoFe-protein. X-ray absorption edge and EXAFS experiments have been carried out at the S, Fe, and MO edges of FeMoco as well as for a number of relevant inorganic cluster complexes. Analysis of EXAFS data has utilized a new approach based on theroetical parameters and multiple scattering analysis (called GNXAS) to provide more reliable information about longer-range interaction in the polynuclear FeMo cluster. Additonal information has been determined about electronic structural changes upon redox chemistry and the binding of exogeneous ligands. X-ray scattering @AS) measurments can be used to investigate the size and shape of molecules in solution. Such XAS studies have been used to probe the structure of FeMoco in solution and how it is altered by redox and ligand-binding. Taken together, these results help provide information on the structural and functional role of the various sub-cluster components of FeMoco. This work is supported by grants from NM and NSF. The x-ray absorption and scattering data were measured at the Stanford Synchrotron Radiation Laboratory which is supported by the U.S. Department of Energy and the NIH.