Holdings: Heme peroxidases :: THWS Bibkatalog

Heme peroxidases:

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Bibliographic Details
Main Author:	Dunford, Hugh Brian (Author)
Format:	Book
Language:	English
Published:	New York [u.a.] Wiley-VCH 1999
Subjects:	Peroxidase Peroxidasen Katalase Häm
Online Access:	Inhaltsverzeichnis
Physical Description:	XIII, 507 S. Ill., graph. Darst.
ISBN:	0471242446

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MARC


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adam_text	^¦H CONTENTS Preface xi 1. Introduction. Historical Background 1 1.1. Heme Prosthetic Group 1 1.2. Role of Peroxidases in the Development of Modern Enzymology 4 1.3. Early Enzyme Kinetics 5 1.4. Some Early Peroxidase Highlights 7 1.5. Post World War II Developments 7 1.6. Relation to Cytochrome c, Myoglobin, Hemoglobin, and Cytochrome P450 12 1.7. Cytochrome c Oxidase 14 1.8. Nobel Prizes 14 2. Model Peroxidases from Yeast and Horseradish, Cloned Enzymes, and Comparison to Metmyoglobin 18 2.1. Introduction 18 2.2. Horseradish Peroxidase 19 2.3. Yeast Cytochrome c Peroxidase 23 2.4. Cloned Enzymes 26 2.5. Comparisons of Horseradish and Yeast Enzymes and Relation to the Globins 26 3. Heme Peroxidase and Catalase Families and Superfamilies: Crystal Structures 33 3.1. Introduction. Structural Basis for Families 33 3.2. Peroxidase Superfamilies 34 3.3. Crystal Structures of Peroxidases and Catalases 37 3.4. Details of the Yeast Cytochrome c Peroxidase Structure 44 3.5. Structures of the Cytochrome c Peroxidase Cytochrome c Complexes 52 v Vi CONTENTS 4. Horseradish Peroxidase. I: Ligand Binding, Redox Potentials, Formation of Its Compounds, and Some of Their Reactions 58 4.1. Isoenzyme C of Horseradish Peroxidase 58 4.2. Ligand Binding to Horseradish Peroxidase 58 4.3. Proton Balance Titrations for Interconversion of Horseradish Peroxidase and Its Compounds 64 4.4. Reduction Potentials of Horseradish Peroxidase and Its Compounds 67 4.5. Mechanism of Peroxidase Compound I Formation 70 4.6. Reactions of Compound I 75 4.7. Reactions of Compound II 82 4.8. Ferrous Peroxidase 85 4.9. Compound III or Oxyperoxidase 86 4.10. Compound X 88 4.11. Alkaline Form of Horseradish Peroxidase 88 5. Horseradish Peroxidase. II: Isoenzymes, Steady State Kinetics, and Peroxidase Oxidase Reaction 92 5.1. Isoenzymes of Horseradish Peroxidase 92 5.2. Steady State Kinetics 93 5.3. Peroxidase Oxidase Reaction 97 5.4. Appendix: Derivation of Steady State Rate Equations 107 6. Horseradish Peroxidase. Ill: Reaction with Indole 3 Acetic Acid, Light Emission, and Quantitative Structure Activity Relationships 112 6.1. Reaction of Horseradish Peroxidase with Indole 3 Acetic Acid 112 6.2. Other Light Emitting Peroxidase Reactions 121 6.3. Quantitative Structure Activity Relationships 128 7. Spectroscopy of Horseradish Peroxidase. I: Optical, Resonance Raman, Magnetic Circular Dichroism, X ray Absorption, and Diffraction 135 7.1. Optical Absorption Spectra 135 7.2. Resonance Raman Spectroscopy 143 7.3. Magnetic Circular Dichroism 154 7.4. X ray Absorption Spectroscopy 165 7.5. X ray Diffraction: Crystal Structure of Horseradish Peroxidase 169 CONTENTS Vii 8. Spectroscopy of Horseradish Peroxidase. II: Nuclear Magnetic Resonance, Electron Paramagnetic Resonance, Electron Nuclear Double Resonance, Mossbauer Spectroscopy, and Theoretical Studies 175 8.1. Nuclear Magnetic Resonance Spectroscopy 175 8.2. Electron Paramagnetic Resonance Spectroscopy 190 8.3. Electron Nuclear Double Resonance Spectroscopy 200 8.4. Mossbauer Spectroscopy 204 8.5. Theoretical Studies 212 9. Yeast Cytochrome c Peroxidase. I: Properties and Reactions with Small Molecules 219 9.1. Introduction 219 9.2. Overview of Properties 220 9.3. Kinetics 231 9.4. Proton Stoichiometry 239 9.5. Site Directed Mutagenesis 240 9.6. Nuclear Magnetic Resonance Spectra 242 9.7. Resonance Raman Spectra 244 9.8. Ferrous Enzyme 245 10. Yeast Cytochrome c Peroxidase. II: Interaction with Cytochrome c 252 10.1. Introduction 252 10.2. Equilibrium Binding to the Native Enzyme 253 10.3. Nuclear Magnetic Resonance Studies 255 10.4. Steady State Kinetics 255 10.5. Transient State Kinetics 259 10.6. Rate of Intracomplex Electron Transfer 260 10.7. Crystal Structures for the Complex 265 10.8. Conclusions 266 11. Other Class I Peroxidases: Ascorbate Peroxidase and Bacterial Catalase Peroxidases 270 11.1. Ascorbate Peroxidase 270 11.2. Bacterial Catalase Peroxidases 276 12. Class II Peroxidases: Lignin, Manganese, and Coprinus cinereus Peroxidases 281 12.1. Lignin Peroxidase 281 12.2. Manganese Peroxidase 295 12.3. Coprinus cinereus (Arthromyces ramosus) Peroxidase 299 ViH CONTENTS 13. Other Class III Plant Peroxidases: Peanut, Barley, Tobacco, and Arabidopsis thaliana 309 13.1. Peanut Peroxidases 309 13.2. Barley Peroxidase 314 13.3. Tobacco Peroxidases 317 13.4. Arabidopsis thaliana Peroxidases 318 13.5. Other Class III Plant Peroxidases 319 13.6. Stereospecific Lignin Biosynthesis 319 13.7. Cancer in Plants 319 14. Chloroperoxidase and Pseudomonas Cytochrome c Peroxidase 323 14.1. Chloroperoxidase 323 14.2. Pseudomonas aeruginosa Cytochrome c Peroxidase 339 15. Myeloperoxidase and Eosinophil Peroxidase: Phagocytosis and Microbial Killing 349 15.1. Discovery of Myeloperoxidase 349 15.2. Preparation and Properties of Myeloperoxidase 350 15.3. Cloning of Myeloperoxidase, Site Directed Mutagenesis 355 15.4. Crystal Structure 356 15.5. Assays for Myeloperoxidase 359 15.6. Reactions of Native Myeloperoxidase 359 15.7. Transient State Kinetics of Myeloperoxidase Reactions 364 15.8. What Is the Chlorinating Reagent in Myeloperoxidase Reactions? 369 15.9. Reactions with Hypochlorous Acid 370 15.10. Reduced Myeloperoxidase and Its Nitrosyl Complex 372 15.11. Steady State Reactions of Myeloperoxidase 372 15.12. Role of Superoxide 373 15.13. Myeloperoxidase Inhibitors and Protectors 374 15.14. Physiological Effects of Myeloperoxidase 375 15.15. Oxygen Burst, Phagocytosis, and Microbial Killing 376 15.16. Hereditary Myeloperoxidase Deficiency 378 15.17. Eosinophil Peroxidase 378 16. Prostaglandin Endoperoxide H Synthases 386 16.1. Introduction 386 16.2. Introduction to Mechanism of Action of Prostaglandin H Synthase 388 16.3. Crystal Structure 396 CONTENTS iX 16.4. Mechanism of Conversion of Arachidonic Acid to Prostaglandin H2 397 16.5. Other Prostaglandin H Synthase Reactions 403 16.6. Discovery of Prostaglandin H Synthase 2 405 16.7. Aspirin and Other NSAID Binding Sites 406 16.8. Nomenclature 407 16.9. Summary 407 16.10. Appendix 407 17. Lactoperoxidase, Thyroid Peroxidase, and Other Animal Peroxidases 414 17.1. Introduction 414 17.2. Bovine Lactoperoxidase 414 17.3. Thyroid Peroxidase 423 17.4. Other Animal Peroxidases 429 17.5. Peroxidase Nomenclature 429 18. Catalases 435 18.1. Introduction 435 18.2. Reactions with Ligands 435 18.3. Compound I Formation and the Catalatic Reaction 435 18.4. Mechanism of the Catalatic Reaction 441 18.5. Compound II Reactions of Catalase 444 18.6. Catalase Reaction with Ethanol 444 18.7. Physiological Role of Catalase 445 18.8. Crystal Structures of Catalases 445 18.9. Summary 451 Appendix 454 Index 476
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discipline	Chemie / Pharmazie Biologie
format	Book
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indexdate	2024-07-09T18:37:04Z
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isbn	0471242446
language	English
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physical	XIII, 507 S. Ill., graph. Darst.
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spelling	Dunford, Hugh Brian Verfasser aut Heme peroxidases H. Brian Dunford New York [u.a.] Wiley-VCH 1999 XIII, 507 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Peroxidase Peroxidasen (DE-588)4045219-0 gnd rswk-swf Katalase (DE-588)4163416-0 gnd rswk-swf Häm (DE-588)4244498-6 gnd rswk-swf Peroxidasen (DE-588)4045219-0 s Häm (DE-588)4244498-6 s Katalase (DE-588)4163416-0 s DE-604 HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=008840038&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis
spellingShingle	Dunford, Hugh Brian Heme peroxidases Peroxidase Peroxidasen (DE-588)4045219-0 gnd Katalase (DE-588)4163416-0 gnd Häm (DE-588)4244498-6 gnd
subject_GND	(DE-588)4045219-0 (DE-588)4163416-0 (DE-588)4244498-6
title	Heme peroxidases
title_auth	Heme peroxidases
title_exact_search	Heme peroxidases
title_full	Heme peroxidases H. Brian Dunford
title_fullStr	Heme peroxidases H. Brian Dunford
title_full_unstemmed	Heme peroxidases H. Brian Dunford
title_short	Heme peroxidases
title_sort	heme peroxidases
topic	Peroxidase Peroxidasen (DE-588)4045219-0 gnd Katalase (DE-588)4163416-0 gnd Häm (DE-588)4244498-6 gnd
topic_facet	Peroxidase Peroxidasen Katalase Häm
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work_keys_str_mv	AT dunfordhughbrian hemeperoxidases

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