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Published on: February 17, 2018
Multiple-Edge XAS Studies of Synthetic Iron-Copper Bridged Molecular Assemblies Relevant to Cytochrome c Oxidase.
Hua Holly Zhang1, Adriano Filipponi, Andrea Di Cicco
1Department of Chemistry, Stanford University, Stanford, California 94305, European Synchrotron Radiation Facility, B.P. 220, F-38043 Grenoble, France, Stanford Synchrotron Radiation Laboratory, Stanford University, Stanford, California 94309, and Department of Chemistry, Harvard University, Cambridge, Massachusetts 02138.
Abstract:
An X-ray absorption spectroscopy study has been carried out at the Fe and Cu K-edges for two bridged molecular assemblies, both of which contain an Fe-X-Cu (X = O(2)(-), OH(-)) bridge unit, some of whose features are relevant to the binuclear site of cytochrome c oxidase. The two complexes [(OEP)Fe-O-Cu(Me(6)tren)](1+) and [(OEP)Fe-(OH)-Cu(Me(5)tren)(OClO(3))](1+) have similar structural fragments around the metal centers except that they differ significantly in the bridge structure (the former contains a linear oxo bridge while the latter has a bent hydroxo bridge). We report a comparative study of these complexes using multiple-scattering (MS) EXAFS analysis and the program package GNXAS. It is found that there is a dramatic increase in the amplitude of the Fe-X-Cu MS pathway as the bridge unit approaches linearity. Full EXAFS MS analysis enables accurate quantitation of bridge metrical details and geometry for both complexes. These studies were done with an expanded version of GNXAS, which allows for simultaneous multiple-edge fitting. Such multiple-edge analysis (using both Fe and Cu edge data) allows common pathways (in this case involving the Fe-X-Cu bridge) to be constrained to be the same, thus improving the observation/variable ratio and enhancing sensitivity for determination of the bridge structure. The accuracy of the structural determination for the bridge units is evaluated by a statistical analysis methodology in which correlations among fitting parameters are identified and contour plots are used to determine random error. The overall error in the EXAFS structural determination is found by establishing the variance with the crystallographically determined values: for the EXAFS-determined parameters at distances below 4 Å, distances and angles deviated on average from crystallographic values by 0.014 Å and 1.5 degrees, respectively. It is also established that structural features in the Fe absorption preedge are diagnostic of oxo vs hydroxo ligation. The relevance of this study to the structural definition of binuclear bridged sites in cytochrome c oxidase and other metalloenzymes is considered.
