Unique cyanide nitrogen-15 nuclear magnetic resonance chemical shift values for cyano-peroxidase complexes. Relevance to the heme active-site structure and mechanism of peroxide activation

  • Behere D
  • Gonzalez-Vergara E
  • Goff H
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Cyanide ion has been utilized to probe the heme environment of the ferric states of horseradish peroxidase, lactoperoxidase and chloroperoxidase. The15N-NMR signal for cyanide bound to these enzymes is located in the downfield region from 578 to 412 ppm (with respect to the nitrate ion reference). The corresponding signal for met-forms of hemoglobin, myoglobin and cytochrome c is much further downfield in the 1047-847 ppm region. The signal position for peroxidases is quite invariant with pH in the physiological ranges. The upfield bias for peroxidase chemical shifts must reflect unique trans iron(III) ligand types and/or proximal-group hydrogen bonding or steric effects. Model compound studies reveal a significant upfield cyanide15N shift with addition of agents capable of hydrogen-bonding to the coordinated cyanide ion. An even more striking upfield shift of 277 ppm is associated with deprotonation of a trans imidazole residue. The distinctive chemical shifts observed for the cyano ligand in peroxidases support the hypothesis that a distal hydrogen-bonding network and perhaps a polar, basic trans ligand are essential for OO bond activation by peroxidases. © 1985.

Author-supplied keywords

  • 15N-NMR
  • Chemical shift
  • Cyanide
  • Heme coordination structure
  • Peroxidase

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