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X-ray absorption edge fine structure spectroscopy of the active site haem of cytochrome c

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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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Author notes

  1. A. LABHARDT

    Present address: Department of Biophysical Chemistry, Biocentre of the University of Basel, Switzerland

Authors and Affiliations

  1. Department of Biochemistry, Stanford University Medical Center, Stanford, California, 94305

    A. LABHARDT

  2. Department of Physics, Stanford University, Stanford, California, 94305

    C. YUEN

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  1. A. LABHARDT
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  2. C. YUEN
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LABHARDT, A., YUEN, C. X-ray absorption edge fine structure spectroscopy of the active site haem of cytochrome c. Nature 277, 150–151 (1979). https://doi.org/10.1038/277150a0

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