عنوان
پدید آورنده
موضوع
رده
QP603.H45
QP603
.
H45
کتابخانه
محل استقرار
1788012917
9781788012911
1782629912
9781782629917
Dioxygen-dependent heme enzymes /
[Book]
editors: Masao Ikeda-Saito, Emma Raven.
Cambridge, England :
Royal Society of Chemistry,
2018.
©2019
1 online resource :
illustrations
Metallobiology Series,
no. 13
2045-5488 ;
Includes bibliographical references and index.
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
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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.
Dioxygen-dependent heme enzymes.
Dioxygen-dependent heme enzymes.
1782629912
9781788012911
Biochemistry.
Heme oxygenase.
Organometallic compounds.
Biochemistry.
Heme oxygenase.
Organometallic compounds.
SCIENCE-- Life Sciences-- Biochemistry.
SCI-- 007000
572/
.
791
23
QP603
.
H45
Ikeda-Saito, Masao
Raven, Emma
20200823053618.0
pn
مطالعه متن کتاب [Book]
Y
