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Model System Studies of Axial Ligation in the Oxidized Reaction States of Cytochrome P-450 Enzymes

  • Chapter
Iron and Copper Proteins

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 74))

Abstract

Cytochrome P-450 enzymes have been isolated from bacteria, microsomes, and mitochondria and catalyze the insertion of one atom of dioxygen into substrate while the other is reduced to water. The biological and many of the physical properties of these enzymes are summarized elsewhere (Hill et al., 1970a; Ullrich, 1972; Gunsalus et al., 1973; Tomaszewski et al., 1974). Substantial clarification of the nature of P-450 dependent oxygenase reactions has been afforded by isolation of the soluble cytochrome (P-450cam) from Pseudomonas putida grown on camphor. In vitro assembly of the of the enzyme system, which also includes an electron transfer chain comprised of a reductase and the 2Fe–2S protein putidaredoxin, has led to deduction of reaction sequence (1) (Tyson et al., 1972; Gunsalus et al., 1973). In this scheme S = substrate, ox = Fe(III), red = Fe(II), and s-red is the one-electron reduction product of the Fe(II)·O2 form. More recently microsomal P-450 cytochromes have been purified and enzyme systems assembled (Imai and Sato, 1974; van der Hoeven and Coon, 1974; Haugen et al., 1975; Guengerich et al., 1975).

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Author information

Authors and Affiliations

  1. Department of Chemistry, Stanford University, Stanford, CA, 94305, USA

    R. H. Holm

  2. Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA

    S. C. Tang & S. Koch

  3. Department of Chemistry, Northwestern University, Evanston, ILL, 60201, USA

    J. A. Ibers

  4. Department of Chemistry, Francis Bitter National Magnet Laboratory, M.I.T., USA

    G. C. Papaefthymiou, S. Foner & R. B. Frankel

Authors
  1. R. H. Holm
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  2. S. C. Tang
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  3. S. Koch
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  4. G. C. Papaefthymiou
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  5. S. Foner
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  6. R. B. Frankel
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  7. J. A. Ibers
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Editor information

Editors and Affiliations

  1. University of Hawaii School of Medicine, Honolulu, Hawaii, USA

    Kerry T. Yasunodu  & Howard F. Mower  & 

  2. Kyoto University Faculty of Medicine, Kyoto, Japan

    Osamu Hayaishi

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© 1976 Plenum Press, New York

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Holm, R.H. et al. (1976). Model System Studies of Axial Ligation in the Oxidized Reaction States of Cytochrome P-450 Enzymes. In: Yasunodu, K.T., Mower, H.F., Hayaishi, O. (eds) Iron and Copper Proteins. Advances in Experimental Medicine and Biology, vol 74. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3270-1_25

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  • DOI: https://doi.org/10.1007/978-1-4684-3270-1_25

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-3272-5

  • Online ISBN: 978-1-4684-3270-1

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