Abstract
THE new technique of extended X-ray absorption fine structure spectroscopy (EXAFS)1 offers promise of detecting small changes in conformation around a central metal atom at the active site of a metalloenzyme, and of relating such changes to the catalytic mechanism. An advantage of EXAFS studies over X-ray diffraction is that they can be carried out in solution at physiological pH where the protein can freely interact with its substrate. We describe here EXAFS measurements aimed at detecting conformational changes during reduction of horse heart cytochrome c.
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