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The Heme Protein P-450 in Oxygen Activation: Carbon Monoxide Inhibition and Photochemical Action Spectroscopy as Tools to Study Its Catalytic Role

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Biological Reactive Intermediates—II

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 136))

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Abstract

Complex membrane-bound multienzyme systems such as the ones located in the endoplasmic reticulum (ER) of liver and other organs or those located predominantly in the inner membranes of the mitochondria of endocrine organs catalyze a variety of oxygenating processes which operate on many different endogenous (e.g. steroids, bile acids) as well as foreign compounds (e.g. drugs, pesticides, toxic chemicals, chemical carcinogens, and other xenobiotics). Atmospheric oxygen, O2, and reducing equivalents, provided by reduced pyridine nucleotides, are co-substrates in these reactions in which, in a formal sense, one or both of the atoms of the oxygen molecule are inserted into the reaction products (monooxygenation and dioxygenation, respectively).

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© 1982 Springer Science+Business Media New York

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Schleyer, H., Hamill, S., Cooper, D.Y., Rosenthal, O. (1982). The Heme Protein P-450 in Oxygen Activation: Carbon Monoxide Inhibition and Photochemical Action Spectroscopy as Tools to Study Its Catalytic Role. In: Snyder, R., et al. Biological Reactive Intermediates—II. Advances in Experimental Medicine and Biology, vol 136. Springer, New York, NY. https://doi.org/10.1007/978-1-4757-0674-1_8

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  • DOI: https://doi.org/10.1007/978-1-4757-0674-1_8

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  • Print ISBN: 978-1-4757-0676-5

  • Online ISBN: 978-1-4757-0674-1

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