Since the discovery of the first examples of 2-oxoglutarate-dependent oxygenase-catalysed reactions in the 1960s, a remarkably broad diversity of alternate reactions and substrates has been revealed, and extensive advances have been achieved in our understanding of the structures and catalytic mechanisms. These enzymes are important agrochemical targets and are being pursued as therapeutic targets for a wide range of diseases including cancer and anemia. This book provides a central source of information that summarizes the key features of the essential group of 2-oxoglutarate-dependent dioxygenases and related enzymes. Given the numerous recent advances and biomedical interest in the field, this book aims to unite the latest research for those already working in the field as well as to provide an introduction for those newly approaching the topic, and for those interested in translating the basic science into medicinal and agricultural benefits. The book begins with four broad chapters that highlight critical aspects, including an overview of possible catalytic reactions, structures and mechanisms. The following seventeen chapters focus on carefully selected topics, each written by leading experts in the area. Readers will find explanations of rapidly evolving research, from the chemistry of isopenicillin N synthase to the oxidation mechanism of 5-methylcytosine in DNA by ten-eleven-translocase oxygenases.

Molecular Mechanisms of Oxygen Activation reviews some of the major advances that have been made in our understanding of the molecular mechanisms underlying oxygen activation, with emphasis on the role of oxygen activation in contemporary biological processes. The biological role of oxygenases in the metabolism of fatty acids and steroids is discussed, along with the functions of heme-containing dioxygenases, a-ketoglutarate-coupled dioxygenases, and pterin-requiring aromatic amino acid hydroxylases. This book is comprised of 14 chapters and begins with an overview of the general properties and biological functions of oxygenases, along with the chemical aspects of oxygen fixation reactions. The reader is then introduced to research concerning fatty acid and steroid oxygenases which has appeared in the literature since 1962, paying particular attention to the mechanism of oxygenation and the biosynthesis and metabolism of steroids. Subsequent chapters explore the biological functions of a variety of oxygenases such as heme-containing dioxygenases, copper-containing oxygenases, flavoprotein oxygenases, and pterin-requiring aromatic amino acid hydroxylases. Superoxide dismutase, cytochrome c oxidase, peroxidase, and bacterial monoxygenases are also considered. This monograph should serve as a valuable reference for biochemists as well as undergraduate and graduate students of biochemistry.

Oxygenases focuses on the processes, methodologies, technologies, and approaches involved in oxygenases, including its distribution in animals, plants, and microorganisms and its role in the metabolism of aromatic, cyclic, and aliphatic compounds. The selection first offers information on the history and scope of oxygenases, methodology of oxygen isotopes, and phenolytic oxygenases. Discussions focus on the separation and purification of compounds for isotopic analysis; general properties and mechanisms of action of oxygenases; physiological significance of oxygenases; dehydrogenases, oxidases, and oxygenases; and problems and restrictions in the use of oxygen-18. The text then examines aromatic hydroxylations, oxygenases in lipid and steroid metabolism, and bacterial oxidation of hydrocarbons. Topics include anaerobic oxidation of alkanes, involvement of molecular oxygen in hydrocarbon utilization, steroid hydroxylation mechanisms, oxygenases in the biosynthesis of steroid hormones, conversion of dopamine to norepinephrine, and general discussion of mechanism of aerobic hydroxylation reactions. The selection is a valuable reference for researchers interested in the process of oxygenases.

Oxygenases: Advances in Research and Application: 2011 Edition is a ScholarlyBrief™ that delivers timely, authoritative, comprehensive, and specialized information about Oxygenases in a concise format. The editors have built Oxygenases: Advances in Research and Application: 2011 Edition on the vast information databases of ScholarlyNews.™ You can expect the information about Oxygenases in this eBook to be deeper than what you can access anywhere else, as well as consistently reliable, authoritative, informed, and relevant. The content of Oxygenases: Advances in Research and Application: 2011 Edition has been produced by the world’s leading scientists, engineers, analysts, research institutions, and companies. All of the content is from peer-reviewed sources, and all of it is written, assembled, and edited by the editors at ScholarlyEditions™ and available exclusively from us. You now have a source you can cite with authority, confidence, and credibility. More information is available at http://www.ScholarlyEditions.com/.

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Oxygenases—Advances in Research and Application: 2013 Edition is a ScholarlyBrief™ that delivers timely, authoritative, comprehensive, and specialized information about ZZZAdditional Research in a concise format. The editors have built Oxygenases—Advances in Research and Application: 2013 Edition on the vast information databases of ScholarlyNews.™ You can expect the information about ZZZAdditional Research in this book to be deeper than what you can access anywhere else, as well as consistently reliable, authoritative, informed, and relevant. The content of Oxygenases—Advances in Research and Application: 2013 Edition has been produced by the world’s leading scientists, engineers, analysts, research institutions, and companies. All of the content is from peer-reviewed sources, and all of it is written, assembled, and edited by the editors at ScholarlyEditions™ and available exclusively from us. You now have a source you can cite with authority, confidence, and credibility. More information is available at http://www.ScholarlyEditions.com/.