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Heme-Thiolate Proteins Different from Cytochromes P450 Catalyzing Monooxygenations

  • Chapter
Cytochrome P450

Abstract

Many hemoproteins involving a histidine proximal iron ligand, like hemoglobins, myoglobins, peroxidases, cytochromes, and prostaglandin synthases, have been found in living organisms.1 On the contrary, only a limited number of hemoprotein families where the heme iron is bound to a cysteinate proximal ligand have been discovered so far. The Fe(II)-CO complex of these hemoproteins is most often characterized by a visible spectrum exhibiting a redshifted Soret peak around 450 nm, which is related to the presence of the very electron-rich cysteinate ligand in trans position to CO.2 This distinctive feature of heme-thiolate proteins has been found so far for only three classes of hemoproteins, the cytochromes P450, nitric oxide synthases, and chloroperoxidase. Another heme-thiolate protein, called protein H450, has been reported, but it remains much less known than the other three. Among these heme-thiolate proteins, the cytochromes P450 responsible for monooxygenation reactions (which will be called “classical P450s” in this chapter) have been extensively studied3 and their mechanisms of dioxygen activation and substrate hydroxylation are now well established.3,4 During these last years, some cytochromes P450 that catalyze reactions very different from monooxygenations have been discovered.5 Moreover, a new class of heme—thiolate proteins, the NO synthases, which are closely related to P450s,6–8 but which would not belong to the P450 superfamily,9 has been discovered. This chapter will focus on these “nonclassical P450s” and on NO synthases, with a special emphasis on a comparison of their biochemical and mechanistic properties with those of the two more classical heme-thiolate ins, the “classical P450s” and the chloroperoxidase from Caldariomyces fumago.

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  1. Jean-Paul Renaud

    Present address: Institut de Génétique et Biologie Moléculaire et Cellulaire, UPR 9004 CNRS, F-67400, Illkirch-Graffenstaden, France

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  1. Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, URA 400 CNRS, Université Paris V, F-75270, Paris Cedex 06, France

    Daniel Mansuy & Jean-Paul Renaud

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  1. Daniel Mansuy
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  2. Jean-Paul Renaud
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  1. Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, 94143, San Francisco, California, USA

    Paul R. Ortiz de Montellano

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Mansuy, D., Renaud, JP. (1995). Heme-Thiolate Proteins Different from Cytochromes P450 Catalyzing Monooxygenations. In: de Montellano, P.R.O. (eds) Cytochrome P450. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2391-5_15

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  • DOI: https://doi.org/10.1007/978-1-4757-2391-5_15

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4419-3248-8

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