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The State of Protonation of the Proximal Histidyl Imidazole in Horseradish Peroxidase

  • Conference paper
The Biological Chemistry of Iron

Part of the book series: NATO Advanced Study Institutes Series ((ASIC,volume 89))

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Abstract

The ease of formation of iron(IV) complexes in horseradish peroxidase as well as in other hemoproteins has been cited to support the view that in these proteins the proximal histidyl imidazole is deprotonated. However, most of the supporting evidence for this proposal has been indirect. From a detailed comparison of the proton nmr spectra of horseradish peroxidase in several oxidation/spin/ligation states with other hemoproteins and model compounds, it is shown hereby direct detection of the N1H signal, that the proximal histidyl imidazole in horseradish peroxidase is definitely not deprotonated, but most likely involved in hydrogen bonding interactions with the protein in at least the reduced and the cyanide-ligated states.

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Author information

Authors and Affiliations

  1. Department of Chemistry, University of California, Davis, California, 95616, USA

    Gerd N. La Mar, V. P. Chacko & Jeffrey S. de Ropp

Authors
  1. Gerd N. La Mar
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  2. V. P. Chacko
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  3. Jeffrey S. de Ropp
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Editor information

Editors and Affiliations

  1. Dept. of Chemistry, University of Alberta, Edmonton, Canada

    H. Brian Dunford

  2. Dept. of Chemistry, University of British Columbia, Vancouver, Canada

    David Dolphin

  3. Dept. of Chemistry, University of California, Berkeley, USA

    Kenneth N. Raymond

  4. Dept. of Molecular Structure, University of Washington, Seattle, USA

    Larry Sieker

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© 1982 D. Reidel Publishing Company

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La Mar, G.N., Chacko, V.P., de Ropp, J.S. (1982). The State of Protonation of the Proximal Histidyl Imidazole in Horseradish Peroxidase. In: Dunford, H.B., Dolphin, D., Raymond, K.N., Sieker, L. (eds) The Biological Chemistry of Iron. NATO Advanced Study Institutes Series, vol 89. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-7882-9_23

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  • DOI: https://doi.org/10.1007/978-94-009-7882-9_23

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-009-7884-3

  • Online ISBN: 978-94-009-7882-9

  • eBook Packages: Springer Book Archive

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