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Models for Horseradish Peroxidase Compound II: Phenol Oxidation with Oxoiron(IV) Porphyrins

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Book cover The Activation of Dioxygen and Homogeneous Catalytic Oxidation

Abstract

The role of iron protoporphyrin (IX), the prosthetic group in most heme proteins, is determined by the local environment of the heme group. Thus in cytochrome b5 it has two tightly bound ligands and it is involved in electron transport. In hemoglobin, cytochrome P450 monooxygenases and peroxidases, however, the sixth (distal) ligand is either absent or only weakly bound allowing ligation of dioxygen or hydrogen peroxide to the metal centre. The behaviour of the latter group of heme proteins is further defined by the nature of the fifth (proximal) ligand and the polarity of and access to the active site.1 Much recent research has been directed towards determining these controlling factors since they have important implications in the understanding of biological systems and in the development of new catalytic oxidations.

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© 1993 Springer Science+Business Media New York

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Colclough, N., Smith, J.R.L. (1993). Models for Horseradish Peroxidase Compound II: Phenol Oxidation with Oxoiron(IV) Porphyrins. In: Barton, D.H.R., Martell, A.E., Sawyer, D.T. (eds) The Activation of Dioxygen and Homogeneous Catalytic Oxidation. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3000-8_13

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  • DOI: https://doi.org/10.1007/978-1-4615-3000-8_13

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6307-1

  • Online ISBN: 978-1-4615-3000-8

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