Peroxidases and Catalases : Biochemistry, Biophysics, Biotechnology and Physiology

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  • Edition: 2nd
  • Format: Hardcover
  • Copyright: 2010-03-15
  • Publisher: Wiley

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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

Prefacep. XIII
Contributorsp. XV
Historical: Pioneering Work on Horseradish and Yeast Cytochrome c Peroxidasesp. 1
Introductionp. 1
Techniques and Instrumentationp. 2
Summary and Conclusionsp. 5
Referencesp. 6
Heme Peroxidase and Catalase Familiesp. 9
Plant, Fungal, and Bacterial Peroxidasesp. 9
Mammalian Peroxidasesp. 11
Catalasesp. 12
Referencesp. 12
Horseradish Peroxidase. I. The Native Enzyme, Compounds I and II, their Structures, and their Cyclep. 13
Introductionp. 13
The Classic Peroxidase Cyclep. 13
Structure and Properties of Native Horseradish Peroxidase Cp. 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 Peroxidasep. 27
Referencesp. 30
Horseradish Peroxidase. II. Two-Electron Reactions, Ferrous Peroxidase, Compound III, The Five Oxidation States, Oxygen Evolution, and Inactivationp. 41
Introductionp. 41
Two-Electron Oxidations By Compound Ip. 41
Oxygen Transfer By One-Electron Mechanismsp. 44
Ferrous Horseradish Peroxidase and Compound IIIp. 45
The Five Oxidation States of Horseradish Peroxidasep. 48
The Catalatic Reactionp. 50
The HRP Clock Reactionp. 51
Enzyme Inactivationp. 51
Referencesp. 52
Horseradish Peroxidase. III. Oscillations and Peroxidase-Oxidase Reactions with NADH, Indole-3-Acetic Acid, And Isobutyraldehyde. Light Emissionp. 57
Oscillations and the NADH Peroxidase-Oxidase Reactionp. 57
Peroxidase Oxidase Reaction with Indole-3-Acetic Acidp. 63
Reaction of Isobutyraldehyde with Horseradish Peroxidasep. 68
Referencesp. 70
Yeast Cytochrome c Peroxidase: Reactions with Small Substratesp. 77
Introductionp. 77
Properties of Yeast Cytochrome c Peroxidasep. 77
Crystal Structures of Yeast Cytochrome c Peroxidase, its Compounds and Complexesp. 78
Mechanism of Compound I Formationp. 80
The Reaction Cycle for Yeast Cytochrome c Peroxidasep. 82
Steady-State Kineticsp. 83
Referencesp. 91
Yeast Cytochrome c Peroxidase: Reaction with Cytochrome cp. 97
Introductionp. 97
Experimental Resultsp. 97
Referencesp. 103
Spectroscopy. I. Optical, Resonance Raman, And X-Ray Absorptionp. 107
Optical Absorption Spectrap. 107
Resonance Raman Spectrap. 111
X-ray Absorption Spectroscopyp. 121
Referencesp. 123
Spectroscopy. II. Nuclear Magnetic Resonance, Electron Spin, and Mössbauerp. 129
Nuclear Magnetic Resonance (NMR) Spectroscopyp. 129
Electron Spin Resonance (ESR) Spectroscopyp. 139
Mössbauer Spectroscopyp. 145
Referencesp. 146
Theoreticalp. 153
Peroxidase Kineticsp. 153
Marcus Theory for Electron Transfer Reactionsp. 156
Electron Tunnelingp. 159
Electron Transfer Reactions in Proteinsp. 160
Electron Density Circuitsp. 161
Diffusion Controlp. 163
Quantum Mechanical Calculationsp. 164
Referencesp. 171
Class I: Ascorbate Peroxidasep. 179
Introductionp. 179
Sequencing and Cloningp. 180
Properties, Reactions, and Intermediate Compoundsp. 181
Crystal Structuresp. 184
Referencesp. 185
Catalase-Peroxidases and Mycobacterium Tuberculosisp. 189
Introductionp. 189
Structures of Catalase-Peroxidasesp. 190
Isoniazid and Other Reactants of Catalase-Peroxidasesp. 192
The Oxidative Defense Mechanisms of Mycobacterium Tuberculosisp. 196
Referencesp. 196
Class II. Lignin, Manganese, Versatile, and Coprinus Cinereus Peroxidasesp. 203
Lignin Peroxidasep. 203
Manganese Peroxidasep. 208
Other Manganese Peroxidases, Versatile Peroxidasep. 210
Coprinus Cinereus (Arthromyces Ramosus) Peroxidasep. 210
Referencesp. 212
Other Class III Peroxidasesp. 221
Arabidopsis Thaliana Peroxidasep. 221
Barley Peroxidasep. 222
Peanut Peroxidasep. 223
Soybean Peroxidasep. 225
Tobacco Peroxidasesp. 225
Turnip Peroxidasesp. 226
Referencesp. 227
Catalasesp. 233
Introductionp. 233
Perspectivep. 234
Progressp. 235
Catalases in Biologyp. 248
Prospectsp. 250
Referencesp. 252
Myeloperoxidase: Enzymologyp. 257
Introductionp. 257
Properties of Myeloperoxidasep. 258
The Compounds of Myeloperoxidasep. 260
Reactions of Myeloperoxidasep. 264
Cloning of Myeloperoxidase: Site-Directed Mutagenesisp. 266
The Crystal Structure and the Prosthetic Group of Myeloperoxidasep. 266
Eosinophil Peroxidasep. 268
Referencesp. 269
Biomedical Aspects of Myeloperoxidase: Halogenation Reactions in Cardiovascular Disease, Infection, and Cancerp. 281
Introductionp. 281
Oxidants Produced by MPO in Humansp. 281
MPO and Coronary Artery Diseasep. 286
MPO and Carcinogenesisp. 288
Prospectsp. 290
Referencesp. 290
Prostaglandin H Synthasep. 297
Introductionp. 297
Crystal Structuresp. 299
Prostaglandin H Synthase-2p. 300
Preliminary Mechanistic Studiesp. 302
Detection of Free Radicals: Role of ESR Spectroscopyp. 303
The Role of Aspirin and Related Substances: Contributions of Vane and Smithp. 304
Work of Marnett and Coworkersp. 305
Work of Kulmacz, Tsai, and Coworkersp. 305
Manganese Prostaglandin Synthasesp. 306
Mechanistic Detailsp. 307
Referencesp. 314
Thyroid Peroxidasep. 323
Introductionp. 323
Hormone Discovery and Chemical Synthesisp. 324
Detection of the Method of Biological Synthesis of Thyroxinep. 325
Conclusionsp. 329
Referencesp. 329
Lacto- and Salivary Peroxidasesp. 335
Introductionp. 335
Propertiesp. 335
The Compounds of Lactoperoxidase and Their Reactionsp. 336
Referencesp. 339
Chloroperoxidase from C. Fumagop. 345
Introductionp. 345
Historyp. 345
Optical Spectrap. 347
ESR, Endor, Mössbauer, Exafs, and Resonance Raman Spectrap. 348
Investigations of Compounds I and IIp. 348
Structure of Compound I and the Catalatic Reactionp. 349
Ligand Bindingp. 350
Kinetics and Mechanisms of Chlorination and Oxidationp. 351
Amino Acid Sequence and Crystal Structurep. 353
Referencesp. 353
Selenium-Containing Enzymes: Glutathione Peroxidase and Iodothyronine Deiodinasep. 359
Introductionp. 359
Glutathione Peroxidasep. 359
Iodothyronine Deiodinasep. 361
Referencesp. 361
Structure and Function of Vanadium Haloperoxidasesp. 363
Summaryp. 363
Abbreviationsp. 364
Introductionp. 364
Occurrence and Biological Function of Vanadium Iodo- and Bromoperoxidasesp. 365
Occurrence and Biological Function of Vanadium Chloroperoxidasesp. 366
Catalytic Properties of Bromoperoxidasep. 367
Properties of the Prosthetic Group in Bromoperoxidasep. 370
Kinetic and Optical Properties of Vanadium Chloroperoxidasesp. 371
Sulfoxidation Reactionsp. 373
Stability of Bromo- and Chloroperoxidasesp. 374
X-ray Structures of Vanadium Bromoperoxidasesp. 374
Active Site of Vanadium Bromoperoxidase From A. Nodosump. 375
X-ray Structures of the Vanadium Chloroperoxidase and Details of the Active Sitep. 376
X-ray Structure of the Peroxo-Intermediate of Vanadium Chloroperoxidase and Difference in Reactivity Between Chloro- and Bromoperoxidasesp. 378
Nature of the Vanadate Cofactorp. 380
Referencesp. 382
Other Heme Peroxidases and Enzymesp. 387
DI-Heme Peroxidasesp. 387
Peroxidases Everywhere You Lookp. 389
Myoglobinsp. 391
Hemoglobinp. 392
Cytochrome c Oxidasep. 392
Oxygenasesp. 392
Heme Oxygenasep. 394
Guanylyl Cyclasep. 394
Referencesp. 395
Application of Peroxidasesp. 403
Introductionp. 403
Background Informationp. 403
Peroxidases as Pharmaceutical and/or Antimicrobial Agentsp. 404
Applications in Bleaching and Detergentsp. 411
Biotransformationsp. 412
Polymerization Reactions and Wastewater Purificationp. 414
Depolymerization Reactionsp. 415
Analytical Applicationsp. 416
Medical Applicationsp. 417
Referencesp. 417
Author Indexp. 425
Subject Indexp. 451
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