Abstract
The application of extended X-ray absorption fine structure (EXAFS) spectroscopy to the structural characterization of the active sites of heme-containing oxygenases and peroxidases is reviewed. Metal-ligand bond distances for first shell atoms can be established to an accuracy of ±0.02 Å and coordination number to ±25%. EXAFS spectroscopy is particularly well suited for establishing the presence of a sulfur donor axial ligand to the heme iron, as is shown to be the case for cytochrome P-450 and chloroperoxidase. In addition, the technique has been used to demonstrate that very short Fe=O bonds (∼ 1.65 Å) are consistently present in high-valent oxo-iron intermediates, such as those in the reaction cycle of horseradish peroxidase. Structural information derived from the use of EXAFS spectroscopy, especially of unstable intermediates for which crystallographic analysis is difficult, provides the foundation for a more thorough understanding of the mechanisms of dioxygen and peroxide activation by heme enzymes.
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Andersson, L.A., Dawson, J.H. (1990). EXAFS Spectroscopy of heme-containing oxygenases and peroxidases. In: Buchler, J.W. (eds) Metal Complexes with Tetrapyrrole Ligands II. Structure and Bonding, vol 74. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-52899-7_1
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