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BL
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| Record Number
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855701
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| Title & Author
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Dioxygen-dependent heme enzymes /\ editors: Masao Ikeda-Saito, Emma Raven.
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| Publication Statement
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Cambridge, England :: Royal Society of Chemistry,, 2018.
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, ©2019
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| Series Statement
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Metallobiology Series,; no. 13
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| Page. NO
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1 online resource :: illustrations
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| ISBN
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1788012917
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: 9781788012911
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1782629912
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9781782629917
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| Bibliographies/Indexes
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Includes bibliographical references and index.
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| Contents
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Cover; Dioxygen-dependent Heme Enzymes; Preface; Biographies; Contents; Section I -- Model Systems; Chapter 1 -- Dioxygen Binding and Activation Mediated by Transition Metal Porphyrinoid Complexes; 1.1 Introduction; 1.2 Role of Transition Metals in Binding and Activating O2; 1.3 Metalloproteins That Bind and Transport O2; 1.4 Activation of O2 by Heme Enzymes; 1.4.1 Heme Monooxygenases; 1.4.1.1 Cytochrome P450; 1.4.1.2 Nitric Oxide Synthase; 1.4.1.3 Heme Oxygenase; 1.4.2 Heme Dioxygenases; 1.4.2.1 Tryptophan 2,3-Dioxygenase (TDO) and Indoleamine 2,3-Dioxygenase (IDO)
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1.5 Metallo-porphyrin and -Porphyrinoid Models for O2 Binding and Activation1.5.1 Iron Complexes; 1.5.1.1 Iron Porphyrins, Phthalocyanines, and Porphyrazines; 1.5.1.2 Iron Corroles and Corrolazines; 1.5.2 Manganese Complexes; 1.5.2.1 Manganese Porphyrins, Phthalocyanines, and Porphyrazines; 1.5.2.2 Manganese Corroles and Corrolazines; 1.6 Summary and Future Directions; Acknowledgements; References; Chapter 2 -- Design and Engineering of Heme Enzymes With O2-dependent Catalytic Activity; 2.1 Introduction; 2.2 Structural and Functional Models of Heme-containing Monooxygenases and Dioxygenases
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2.2.1 The Biological Function of the Cytochrome P450 Monooxygenases2.2.2 The Active Site and Catalytic Cycle of the Cytochrome P450 Monooxygenases; 2.3 Recent Designs that Utilize Alanine Scanning; 2.4 Semi-rational and Rational Design of the P450 Enzymes; 2.5 P450s as a Model for Dioxygen Activation; 2.6 Heme Dioxygenases; 2.7 Functional Models of the Heme-containing Oxidases; 2.7.1 Biological Functions of Terminal Oxidases; 2.7.2 Structure of Heme-Copper Oxidases; 2.7.3 Biosynthetic Models of Heme-Copper Oxidase in Myoglobin; 2.7.3.1 Functional Model of a Heme-Copper Center in a Mb Scaffold
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2.7.3.2 Fine Tuning the Oxidase Activity with Non-native Heme Cofactors2.7.3.3 The Role of Non-heme Metal in Promoting O-O Bond Cleavage; 2.7.3.4 Non-covalent Interactions in Tuning the Reduction Potential and Proton Transfer; 2.7.3.5 Defining the Role of the Active Site Tyrosine by Genetic Incorporation of Tyrosine Analogs; 2.7.3.6 Improving the Oxidase Activity by Optimization of Interfacial Electron Transfer; 2.7.4 Oxygen Activation by de novo Designed Heme Proteins; 2.7.4.1 De novo Designed Heme-binding Maquettes; 2.7.4.2 Oxygen Binding and Activation by Cytochrome c Maquettes
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2.7.4.3 Heme Oxygenase Activity of Heme-binding Maquettes2.7.4.4 Electrocatalytic Oxygen Reduction by Mimochromes; 2.8 Heme-binding DNA/RNAzymes; 2.8.1 Heme-binding Aptamers with Oxidase Activity; 2.8.2 Scope of Oxidation Activity by Heme-binding DNA/RNAzymes; 2.9 Conclusions and Future Perspectives; Acknowledgements; References; Chapter 3 -- Myoglobin Derivatives Reconstituted with Modified Metal Porphyrinoids as Structural and Functional Models of the Cytochrome P450 Enzymes; 3.1 Introduction; 3.2 Reconstitution of Hemoproteins
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| Abstract
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This book highlights the many and varied catalytic activities of O2-dependent heme-iron enzymes, including monoxygenases and cytochrome P450, dioxygenases, oxidases and model heme systems required for postgraduate students and researchers in biochemistry and metallobiology.
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| Subject
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Biochemistry.
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Heme oxygenase.
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Organometallic compounds.
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Biochemistry.
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Heme oxygenase.
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Organometallic compounds.
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| Subject
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SCIENCE-- Life Sciences-- Biochemistry.
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| Dewey Classification
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572/.791
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| LC Classification
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QP603.H45
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| Added Entry
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Ikeda-Saito, Masao
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Raven, Emma
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