Peroxidases and Catalases: Biochemistry, Biophysics, Biotechnology and Physiology

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.

Table of Contents:
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

About the Author :
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.