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Monooxygenase, Peroxidase and Peroxygenase Properties and Mechanisms of Cytochrome P450

Part of the Advances in Experimental Medicine and Biology Book Series (volume 851)

Editors: Hrycay, Eugene G.; Bandiera, Stelvio M.

DOI: 10.1007/978-3-319-16009-2

ISBN: 978-3-319-16008-5

Publisher: Springer International Publishing - Springer Journals

Feb 10, 2015

1 - 10 of 13 Chapters

LitStream

Chapter 1Monooxygenase, Peroxidase and Peroxygenase Properties and Reaction Mechanisms of Cytochrome P450 Enzymes

Hrycay, Eugene G.; Bandiera, Stelvio M.

Pages: 1 –61

[This review examines the monooxygenase, peroxidase and peroxygenase properties and reaction mechanisms of cytochrome P450 (CYP) enzymes in bacterial, archaeal and mammalian systems. CYP enzymes catalyze monooxygenation reactions by inserting one oxygen atom from O2 into an enormous number and...
LitStream

Chapter 2Oxidizing Intermediates in P450 Catalysis: A Case for Multiple Oxidants

Modi, Anuja R.; Dawson, John H.

Pages: 63 –81

[Cytochrome P450 (P450 or CYP) catalysis involves the oxygenation of organic compounds via a series of catalytic intermediates, namely, the ferric-peroxo, ferric-hydroperoxo, Compound I (Cpd I) and FeIII−(H2O2) intermediates. Now that the structures of P450 enzymes have been well established, a...
LitStream

Chapter 3Current Approaches for Investigating and Predicting Cytochrome P450 3A4-Ligand Interactions

Sevrioukova, Irina F.; Poulos, Thomas L.

Pages: 83 –105

[Cytochrome P450 3A4 (CYP3A4) is the major and most important drug-metabolizing enzyme in humans that oxidizes and clears over a half of all administered pharmaceuticals. This is possible because CYP3A4 is promiscuous with respect to substrate binding and has the ability to catalyze diverse...
LitStream

Chapter 4Acyl-Carbon Bond Cleaving Cytochrome P450 Enzymes: CYP17A1, CYP19A1 and CYP51A1

Akhtar, Muhammad; Wright, J. Neville

Pages: 107 –130

[Cytochrome P450 (P450 or CYP) enzymes in their resting state contain the heme-iron in a high-spin FeIII state. Binding of a substrate to a P450 enzyme allows transfer of the first electron, producing a FeII species that reacts with oxygen to generate a low-spin iron superoxide intermediate...
LitStream

Chapter 5Regioselective Versatility of Monooxygenase Reactions Catalyzed by CYP2B6 and CYP3A4: Examples with Single Substrates

Erratico, Claudio A.; Deo, Anand K.; Bandiera, Stelvio M.

Pages: 131 –149

[Hepatic microsomal cytochrome P450 (CYP) enzymes have broad and overlapping substrate specificity and catalyze a variety of monooxygenase reactions, including aliphatic and aromatic hydroxylations, N-hydroxylations, oxygenations of heteroatoms (N, S, P and I), alkene and arene epoxidations,...
LitStream

Chapter 6Cytochrome P450 Enzymes in the Bioactivation of Polyunsaturated Fatty Acids and Their Role in Cardiovascular Disease

Westphal, Christina; Konkel, Anne; Schunck, Wolf-Hagen

Pages: 151 –187

[Various members of the cytochrome P450 (CYP) superfamily have the capacity of metabolizing omega-6 and omega-3 polyunsaturated fatty acids (n-6 and n-3 PUFAs). In most mammalian tissues, CYP2C and CYP2J enzymes are the major PUFA epoxygenases, whereas CYP4A and CYP4F subfamily members function...
LitStream

Chapter 7Monooxygenation of Small Hydrocarbons Catalyzed by Bacterial Cytochrome P450s

Shoji, Osami; Watanabe, Yoshihito

Pages: 189 –208

[Cytochrome P450s (P450s) catalyze the NAD(P)H/O2-dependent monooxygenation of less reactive organic molecules under mild conditions. The catalytic activity of bacterial P450s is very high compared with P450s isolated from animals and plants, and the substrate specificity of bacterial P450s is...
LitStream

Chapter 8Use of Chemical Auxiliaries to Control P450 Enzymes for Predictable Oxidations at Unactivated C-H Bonds of Substrates

Auclair, Karine; Polic, Vanja

Pages: 209 –228

[Cytochrome P450 enzymes (P450s) have the ability to oxidize unactivated C-H bonds of substrates with remarkable regio- and stereoselectivity. Comparable selectivity for chemical oxidizing agents is typically difficult to achieve. Hence, there is an interest in exploiting P450s as potential...
LitStream

Chapter 9Cytochrome P450 Enzymes and Electrochemistry: Crosstalk with Electrodes as Redox Partners and Electron Sources

Shumyantseva, Victoria V.; Bulko, Tatiana; Shich, Evgeniya; Makhova, Anna; Kuzikov, Alexey; Archakov, Alexander

Pages: 229 –246

[The functional significance of cytochrome P450 (P450) enzymes includes their ability to catalyze the biotransformation of xenobiotics (foreign compounds) and endogenous compounds. P450 enzymes play an important role in the detoxification of exogenous bioactive compounds and hydrophobic...
LitStream

Chapter 10Mechanistic Basis of Electron Transfer to Cytochromes P450 by Natural Redox Partners and Artificial Donor Constructs

Hlavica, Peter

Pages: 247 –297

[Cytochromes P450 (P450s) are hemoproteins catalyzing oxidative biotransformation of a vast array of natural and xenobiotic compounds. Reducing equivalents required for dioxygen cleavage and substrate hydroxylation originate from different redox partners including diflavin reductases,...

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