Heme peroxidases:
Gespeichert in:
| 1. Verfasser: | |
|---|---|
| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
New York [u.a.]
Wiley-VCH
1999
|
| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XIII, 507 S. Ill., graph. Darst. |
| ISBN: | 0471242446 |
Internformat
MARC
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| 100 | 1 | |a Dunford, Hugh Brian |e Verfasser |4 aut | |
| 245 | 1 | 0 | |a Heme peroxidases |c H. Brian Dunford |
| 264 | 1 | |a New York [u.a.] |b Wiley-VCH |c 1999 | |
| 300 | |a XIII, 507 S. |b Ill., graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 650 | 4 | |a Peroxidase | |
| 650 | 0 | 7 | |a Peroxidasen |0 (DE-588)4045219-0 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Katalase |0 (DE-588)4163416-0 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Häm |0 (DE-588)4244498-6 |2 gnd |9 rswk-swf |
| 689 | 0 | 0 | |a Peroxidasen |0 (DE-588)4045219-0 |D s |
| 689 | 0 | 1 | |a Häm |0 (DE-588)4244498-6 |D s |
| 689 | 0 | 2 | |a Katalase |0 (DE-588)4163416-0 |D s |
| 689 | 0 | |5 DE-604 | |
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| 999 | |a oai:aleph.bib-bvb.de:BVB01-008840038 | ||
Datensatz im Suchindex
| _version_ | 1804127672222089216 |
|---|---|
| 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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| illustrated | Illustrated |
| indexdate | 2024-07-09T18:37:04Z |
| institution | BVB |
| isbn | 0471242446 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-008840038 |
| oclc_num | 39323127 |
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| owner_facet | DE-20 DE-526 |
| physical | XIII, 507 S. Ill., graph. Darst. |
| publishDate | 1999 |
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| publisher | Wiley-VCH |
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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 |
| url | 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 |
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