EXAFS STUDY OF ACTIVE INTERMEDIATES : HEME ENZYMES AND MODEL COMPOUNDSReport as inadecuate




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Abstract : The iron coordination structures of the oxygenated cytochrome P-450-CAM and chloroperoxidase and of a number of penta- and hexa-coordinate ferrous porphyrin complexes containing biologically relevant, sulfur axial ligands have been investigatied by EXAFS spectroscopy. The two oxygenated enzymes have both been found to contain a sulfur atom located 2.37 Å from the central heme iron. In the CO-ligated series of model complexes, two distinct categories of Fe-Sax distances have been observed that correlate with thiolate and non-thiolate ligation ~2.33 and ~2.41 Å, respectively . The data for these model ferrous-CO ccomplexes, together with previously reported Fe-S distance in oxygenated heme iron model complexes ; allows the sulfur atoms in oxygenated P-450-CAM and chloroperoxidase to be identified as a thiolate sulfur.





Author: Lung-Shan Kau E. Svastits M. Sono J. Dawson K. Hodgson

Source: https://hal.archives-ouvertes.fr/



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