Dioxygen-dependent heme enzymes

Description

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. Abstract: 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.  Read more... Content: 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) 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 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 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 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