Peroxidases and Catalases
John Wiley & Sons Inc (Verlag)
978-0-470-22476-2 (ISBN)
SINGLE SOURCE GUIDE TO PEROXIDASES AND CATALASES
Reflecting the important historical discoveries and exciting research in the field in recent years, Peroxidases and Catalases: Biochemistry, Biophysics, Biotechnology and Physiology provides a much-needed systematic, up-to-date treatment of peroxidases and catalases.
From the structure and properties of the various superfamilies to current applications of peroxidases, the book consolidates vast amounts of information previously scattered in the professional literature, covering all aspects of these ubiquitous enzymes that act on a variety of substances and processes in living systems—their properties, reactions, crystal structures, cloning, and more.
Considering the subject from both theoretical and applied perspectives, Peroxidases and Catalases offers a critical review of the literature and detailed discussions of the most current research. Chapters cover:
The background and history of peroxidases and catalases
Plant, fungal, and bacterial peroxidase superfamilies and their organization
Mammalian peroxidases including medical and physiological roles
Spectroscopic and theoretical techniques for studying peroxidases highlighting the contributions of physicists and physical/theoretical chemists
Heme peroxidases, catalases, and other peroxidases such as vanadium and selenium peroxidase
Relevant plant and animal physiology
This one-stop reference is a vital reference for biochemists, biologists, biochemical engineers, physiologists, environmental and pharmaceutical researchers, and others interested in the study and use of peroxidases and catalases.
H. BRIAN DUNFORD, PHD, is a biophysical chemist currently working on peroxidase enzymes and Professor Emeritus at the University of Alberta. He received his PhD from McGill University. He is the author of Heme Peroxidases, editor of other books, as well as coauthor of more than 250 journal articles.
Preface xiii
Contributors xv
1 Historical: Pioneering Work on Horseradish and Yeast Cytochrome c Peroxidases 1
Introduction 1
Techniques and Instrumentation 2
Summary and Conclusions 5
References 6
2 Heme Peroxidase and Catalase Families 9
Plant, Fungal, and Bacterial Peroxidases 9
Mammalian Peroxidases 11
Catalases 12
References 12
3 Horseradish Peroxidase. I. The Native Enzyme, Compounds I and II, Their Structures, and Their Cycle 13
Introduction 13
The Classic Peroxidase Cycle 13
Structure and Properties of Native Horseradish Peroxidase C 18
Horseradish Peroxidase Compound I (HRP-I) 23
Horseradish Peroxidase Compound II (HRP-II) 26
Some Diverse Approaches to an Understanding of Horseradish Peroxidase 27
References 30
4 Horseradish Peroxidase. II. Two-Electron Reactions, Ferrous Peroxidase, Compound III, The Five Oxidation States, Oxygen Evolution, and Inactivation 41
Introduction 41
Two-Electron Oxidations By Compound I 41
Oxygen Transfer By One-Electron Mechanisms 44
Ferrous Horseradish Peroxidase and Compound III 45
The Five Oxidation States of Horseradish Peroxidase 48
The Catalatic Reaction 50
The HRP Clock Reaction 51
Enzyme Inactivation 51
References 52
5 Horseradish Peroxidase. III. Oscillations and Peroxidase-Oxidase Reactions with NADH, Indole-3- Acetic Acid, and Isobutyraldehyde. Light Emission 57
Oscillations and the NADH Peroxidase-Oxidase Reaction 57
Peroxidase Oxidase Reaction with Indole-3-Acetic Acid 63
Reaction of Isobutyraldehyde with Horseradish Peroxidase 68
References 70
6 Yeast Cytochrome c Peroxidase: Reactions with Small Substrates 77
Introduction 77
Properties of Yeast Cytochrome c Peroxidase 77
Crystal Structures of Yeast Cytochrome c Peroxidase, its Compounds and Complexes 78
Mechanism of Compound I Formation 80
The Reaction Cycle for Yeast Cytochrome c Peroxidase 82
Steady-State Kinetics 83
References 91
7 Yeast Cytochrome c Peroxidase: Reaction with Cytochrome c 97
Introduction 97
Experimental Results 97
References 103
8 Spectroscopy. I. Optical, Resonance Raman, and X-Ray Absorption 107
Optical Absorption Spectra 107
Resonance Raman Spectra 111
X-ray Absorption Spectroscopy 121
References 123
9 Spectroscopy. II. Nuclear Magnetic Resonance, Electron Spin, and MöSsbauer 129
Nuclear Magnetic Resonance (NMR) Spectroscopy 129
Electron Spin Resonance (ESR) Spectroscopy 139
Mössbauer Spectroscopy 145
References 146
10 Theoretical 153
Peroxidase Kinetics 153
Marcus Theory for Electron Transfer Reactions 156
Electron Tunneling 159
Electron Transfer Reactions in Proteins 160
Electron Density Circuits 161
Diffusion Control 163
Quantum Mechanical Calculations 164
References 171
11 Class I: Ascorbate Peroxidase 179
Introduction 179
Sequencing and Cloning 180
Properties, Reactions, and Intermediate Compounds 181
Crystal Structures 184
References 185
12 Catalase-Peroxidases and Mycobacterium Tuberculosis 189
Introduction 189
Structures of Catalase-Peroxidases 190
Isoniazid and Other Reactants of Catalase-Peroxidases 192
The Oxidative Defense Mechanisms of Mycobacterium Tuberculosis 196
References 196
13 Class II. Lignin, Manganese, Versatile, and Coprinus Cinereus Peroxidases 203
Lignin Peroxidase 203
Manganese Peroxidase 208
Other Manganese Peroxidases, Versatile Peroxidase 210
Coprinus Cinereus (Arthromyces Ramosus) Peroxidase 210
References 212
14 Other Class III Peroxidases 221
Arabidopsis Thaliana Peroxidase 221
Barley Peroxidase 222
Peanut Peroxidase 223
Soybean Peroxidase 225
Tobacco Peroxidases 225
Turnip Peroxidases 226
References 227
15 Catalases 233
Peter Jones
Introduction 233
Perspective 234
Progress 235
Catalases in Biology 248
Prospects 250
References 252
16 Myeloperoxidase: Enzymology 257
Introduction 257
Properties of Myeloperoxidase 258
The Compounds of Myeloperoxidase 260
Reactions of Myeloperoxidase 264
Cloning of Myeloperoxidase: Site-Directed Mutagenesis 266
The Crystal Structure and the Prosthetic Group of Myeloperoxidase 266
Eosinophil Peroxidase 268
References 269
17 Biomedical Aspects of Myeloperoxidase: Halogenation Reactions In Cardiovascular Disease, Infection, And Cancer 281
Jeffrey P. Henderson and Jay. W. Heinecke
Introduction 281
Oxidants Produced by MPO in Humans 281
MPO and Coronary Artery Disease 286
MPO and Carcinogenesis 288
Prospects 290
References 290
18 Prostaglandin H Synthase 297
Introduction 297
Crystal Structures 299
Prostaglandin H Synthase-2 300
Preliminary Mechanistic Studies 302
Detection of Free Radicals: Role of ESR Spectroscopy 303
The Role of Aspirin and Related Substances: Contributions of Vane and Smith 304
Work of Marnett and Coworkers 305
Work of Kulmacz, Tsai, and Coworkers 305
Manganese Prostaglandin Synthases 306
Mechanistic Details 307
References 314
19 Thyroid Peroxidase 323
Introduction 323
Hormone Discovery and Chemical Synthesis 324
Detection of the Method of Biological Synthesis of Thyroxine 325
Conclusions 329
References 329
20 Lacto- And Salivary Peroxidases 335
Introduction 335
Properties 335
The Compounds of Lactoperoxidase and Their Reactions 336
References 339
21 Chloroperoxidase From C. Fumago 345
Introduction 345
History 345
Optical Spectra 347
ESR, Endor, Mössbauer, Exafs, and Resonance Raman Spectra 348
Investigations of Compounds I and II 348
Structure of Compound I and the Catalatic Reaction 349
Ligand Binding 350
Kinetics and Mechanisms of Chlorination and Oxidation 351
Amino Acid Sequence and Crystal Structure 353
References 353
22 Selenium-Containing Enzymes: Glutathione Peroxidase and Iodothyronine Deiodinase 359
Introduction 359
Glutathione Peroxidase 359
Iodothyronine Deiodinase 361
References 361
23 Structure and Function of Vanadium Haloperoxidases 363
Ron Wever and Rokus Renirie
Summary 363
Abbreviations 364
Introduction 364
Occurrence and Biological Function of Vanadium Iodo- and Bromoperoxidases 365
Occurrence and Biological Function of Vanadium Chloroperoxidases 366
Catalytic Properties of Bromoperoxidase 367
Properties of the Prosthetic Group in Bromoperoxidase 370
Kinetic and Optical Properties of Vanadium Chloroperoxidases 371
Sulfoxidation Reactions 373
Stability of Bromo- and Chloroperoxidases 374
X-ray Structures of Vanadium Bromoperoxidases 374
Active Site of Vanadium Bromoperoxidase From A. Nodosum 375
X-ray Structures of the Vanadium Chloroperoxidase and Details of the Active Site 376
X-ray Structure of the Peroxo-Intermediate of Vanadium Chloroperoxidase and Difference in Reactivity Between Chloro- and Bromoperoxidases 378
Nature of the Vanadate Cofactor 380
References 382
24 Other Heme Peroxidases and Enzymes 387
DI-Heme Peroxidases 387
Peroxidases Everywhere You Look 389
Myoglobins 391
Hemoglobin 392
Cytochrome c Oxidase 392
Oxygenases 392
Heme Oxygenase 394
Guanylyl Cyclase 394
References 395
25 Application of Peroxidases 403
Ron Wever
Introduction 403
Background Information 403
Peroxidases as Pharmaceutical and/or Antimicrobial Agents 404
Applications in Bleaching and Detergents 411
Biotransformations 412
Polymerization Reactions and Wastewater Purification 414
Depolymerization Reactions 415
Analytical Applications 416
Medical Applications 417
References 417
Author Index 425
Subject Index 451
| Verlagsort | New York |
|---|---|
| Sprache | englisch |
| Maße | 163 x 241 mm |
| Gewicht | 776 g |
| Themenwelt | Naturwissenschaften ► Biologie ► Biochemie |
| Naturwissenschaften ► Chemie ► Organische Chemie | |
| Naturwissenschaften ► Physik / Astronomie ► Angewandte Physik | |
| ISBN-10 | 0-470-22476-2 / 0470224762 |
| ISBN-13 | 978-0-470-22476-2 / 9780470224762 |
| Zustand | Neuware |
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