Peroxidases and Catalases Biochemistry, Biophysics, Biotechnology and Physiology

by Dunford, H. Brian

• ISBN13: 9780470224762
• ISBN10: 0470224762
• Edition: 2nd
• Format: Hardcover
• Copyright: 2010-03-15
• Publisher: Wiley

Summary

Single source guide to peroxidases and catalasesReflecting 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 catalasesPlant, fungal, and bacterial peroxidase superfamilies and their organizationMammalian peroxidases including medical and physiological rolesSpectroscopic and theoretical techniques for studying peroxidases highlighting the contributions of physicists and physical/theoretical chemistsHeme peroxidases, catalases, and other peroxidases such as vanadium and selenium peroxidaseRelevant plant and animal physiologyThis 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.

Author Biography

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.

Table of Contents

Preface	p. XIII
Contributors	p. XV
Historical: Pioneering Work on Horseradish and Yeast Cytochrome c Peroxidases	p. 1
Introduction	p. 1
Techniques and Instrumentation	p. 2
Summary and Conclusions	p. 5
References	p. 6
Heme Peroxidase and Catalase Families	p. 9
Plant, Fungal, and Bacterial Peroxidases	p. 9
Mammalian Peroxidases	p. 11
Catalases	p. 12
References	p. 12
Horseradish Peroxidase. I. The Native Enzyme, Compounds I and II, their Structures, and their Cycle	p. 13
Introduction	p. 13
The Classic Peroxidase Cycle	p. 13
Structure and Properties of Native Horseradish Peroxidase C	p. 18
Horseradish Peroxidase Compound I (HRP-I)	p. 23
Horseradish Peroxidase Compound II (HRP-II)	p. 26
Some Diverse Approaches to an Understanding of Horseradish Peroxidase	p. 27
References	p. 30
Horseradish Peroxidase. II. Two-Electron Reactions, Ferrous Peroxidase, Compound III, The Five Oxidation States, Oxygen Evolution, and Inactivation	p. 41
Introduction	p. 41
Two-Electron Oxidations By Compound I	p. 41
Oxygen Transfer By One-Electron Mechanisms	p. 44
Ferrous Horseradish Peroxidase and Compound III	p. 45
The Five Oxidation States of Horseradish Peroxidase	p. 48
The Catalatic Reaction	p. 50
The HRP Clock Reaction	p. 51
Enzyme Inactivation	p. 51
References	p. 52
Horseradish Peroxidase. III. Oscillations and Peroxidase-Oxidase Reactions with NADH, Indole-3-Acetic Acid, And Isobutyraldehyde. Light Emission	p. 57
Oscillations and the NADH Peroxidase-Oxidase Reaction	p. 57
Peroxidase Oxidase Reaction with Indole-3-Acetic Acid	p. 63
Reaction of Isobutyraldehyde with Horseradish Peroxidase	p. 68
References	p. 70
Yeast Cytochrome c Peroxidase: Reactions with Small Substrates	p. 77
Introduction	p. 77
Properties of Yeast Cytochrome c Peroxidase	p. 77
Crystal Structures of Yeast Cytochrome c Peroxidase, its Compounds and Complexes	p. 78
Mechanism of Compound I Formation	p. 80
The Reaction Cycle for Yeast Cytochrome c Peroxidase	p. 82
Steady-State Kinetics	p. 83
References	p. 91
Yeast Cytochrome c Peroxidase: Reaction with Cytochrome c	p. 97
Introduction	p. 97
Experimental Results	p. 97
References	p. 103
Spectroscopy. I. Optical, Resonance Raman, And X-Ray Absorption	p. 107
Optical Absorption Spectra	p. 107
Resonance Raman Spectra	p. 111
X-ray Absorption Spectroscopy	p. 121
References	p. 123
Spectroscopy. II. Nuclear Magnetic Resonance, Electron Spin, and Mössbauer	p. 129
Nuclear Magnetic Resonance (NMR) Spectroscopy	p. 129
Electron Spin Resonance (ESR) Spectroscopy	p. 139
Mössbauer Spectroscopy	p. 145
References	p. 146
Theoretical	p. 153
Peroxidase Kinetics	p. 153
Marcus Theory for Electron Transfer Reactions	p. 156
Electron Tunneling	p. 159
Electron Transfer Reactions in Proteins	p. 160
Electron Density Circuits	p. 161
Diffusion Control	p. 163
Quantum Mechanical Calculations	p. 164
References	p. 171
Class I: Ascorbate Peroxidase	p. 179
Introduction	p. 179
Sequencing and Cloning	p. 180
Properties, Reactions, and Intermediate Compounds	p. 181
Crystal Structures	p. 184
References	p. 185
Catalase-Peroxidases and Mycobacterium Tuberculosis	p. 189
Introduction	p. 189
Structures of Catalase-Peroxidases	p. 190
Isoniazid and Other Reactants of Catalase-Peroxidases	p. 192
The Oxidative Defense Mechanisms of Mycobacterium Tuberculosis	p. 196
References	p. 196
Class II. Lignin, Manganese, Versatile, and Coprinus Cinereus Peroxidases	p. 203
Lignin Peroxidase	p. 203
Manganese Peroxidase	p. 208
Other Manganese Peroxidases, Versatile Peroxidase	p. 210
Coprinus Cinereus (Arthromyces Ramosus) Peroxidase	p. 210
References	p. 212
Other Class III Peroxidases	p. 221
Arabidopsis Thaliana Peroxidase	p. 221
Barley Peroxidase	p. 222
Peanut Peroxidase	p. 223
Soybean Peroxidase	p. 225
Tobacco Peroxidases	p. 225
Turnip Peroxidases	p. 226
References	p. 227
Catalases	p. 233
Introduction	p. 233
Perspective	p. 234
Progress	p. 235
Catalases in Biology	p. 248
Prospects	p. 250
References	p. 252
Myeloperoxidase: Enzymology	p. 257
Introduction	p. 257
Properties of Myeloperoxidase	p. 258
The Compounds of Myeloperoxidase	p. 260
Reactions of Myeloperoxidase	p. 264
Cloning of Myeloperoxidase: Site-Directed Mutagenesis	p. 266
The Crystal Structure and the Prosthetic Group of Myeloperoxidase	p. 266
Eosinophil Peroxidase	p. 268
References	p. 269
Biomedical Aspects of Myeloperoxidase: Halogenation Reactions in Cardiovascular Disease, Infection, and Cancer	p. 281
Introduction	p. 281
Oxidants Produced by MPO in Humans	p. 281
MPO and Coronary Artery Disease	p. 286
MPO and Carcinogenesis	p. 288
Prospects	p. 290
References	p. 290
Prostaglandin H Synthase	p. 297
Introduction	p. 297
Crystal Structures	p. 299
Prostaglandin H Synthase-2	p. 300
Preliminary Mechanistic Studies	p. 302
Detection of Free Radicals: Role of ESR Spectroscopy	p. 303
The Role of Aspirin and Related Substances: Contributions of Vane and Smith	p. 304
Work of Marnett and Coworkers	p. 305
Work of Kulmacz, Tsai, and Coworkers	p. 305
Manganese Prostaglandin Synthases	p. 306
Mechanistic Details	p. 307
References	p. 314
Thyroid Peroxidase	p. 323
Introduction	p. 323
Hormone Discovery and Chemical Synthesis	p. 324
Detection of the Method of Biological Synthesis of Thyroxine	p. 325
Conclusions	p. 329
References	p. 329
Lacto- and Salivary Peroxidases	p. 335
Introduction	p. 335
Properties	p. 335
The Compounds of Lactoperoxidase and Their Reactions	p. 336
References	p. 339
Chloroperoxidase from C. Fumago	p. 345
Introduction	p. 345
History	p. 345
Optical Spectra	p. 347
ESR, Endor, Mössbauer, Exafs, and Resonance Raman Spectra	p. 348
Investigations of Compounds I and II	p. 348
Structure of Compound I and the Catalatic Reaction	p. 349
Ligand Binding	p. 350
Kinetics and Mechanisms of Chlorination and Oxidation	p. 351
Amino Acid Sequence and Crystal Structure	p. 353
References	p. 353
Selenium-Containing Enzymes: Glutathione Peroxidase and Iodothyronine Deiodinase	p. 359
Introduction	p. 359
Glutathione Peroxidase	p. 359
Iodothyronine Deiodinase	p. 361
References	p. 361
Structure and Function of Vanadium Haloperoxidases	p. 363
Summary	p. 363
Abbreviations	p. 364
Introduction	p. 364
Occurrence and Biological Function of Vanadium Iodo- and Bromoperoxidases	p. 365
Occurrence and Biological Function of Vanadium Chloroperoxidases	p. 366
Catalytic Properties of Bromoperoxidase	p. 367
Properties of the Prosthetic Group in Bromoperoxidase	p. 370
Kinetic and Optical Properties of Vanadium Chloroperoxidases	p. 371
Sulfoxidation Reactions	p. 373
Stability of Bromo- and Chloroperoxidases	p. 374
X-ray Structures of Vanadium Bromoperoxidases	p. 374
Active Site of Vanadium Bromoperoxidase From A. Nodosum	p. 375
X-ray Structures of the Vanadium Chloroperoxidase and Details of the Active Site	p. 376
X-ray Structure of the Peroxo-Intermediate of Vanadium Chloroperoxidase and Difference in Reactivity Between Chloro- and Bromoperoxidases	p. 378
Nature of the Vanadate Cofactor	p. 380
References	p. 382
Other Heme Peroxidases and Enzymes	p. 387
DI-Heme Peroxidases	p. 387
Peroxidases Everywhere You Look	p. 389
Myoglobins	p. 391
Hemoglobin	p. 392
Cytochrome c Oxidase	p. 392
Oxygenases	p. 392
Heme Oxygenase	p. 394
Guanylyl Cyclase	p. 394
References	p. 395
Application of Peroxidases	p. 403
Introduction	p. 403
Background Information	p. 403
Peroxidases as Pharmaceutical and/or Antimicrobial Agents	p. 404
Applications in Bleaching and Detergents	p. 411
Biotransformations	p. 412
Polymerization Reactions and Wastewater Purification	p. 414
Depolymerization Reactions	p. 415
Analytical Applications	p. 416
Medical Applications	p. 417
References	p. 417
Author Index	p. 425
Subject Index	p. 451
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