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 xiiiContributors xv1 Historical: Pioneering Work on Horseradish and Yeast Cytochrome c Peroxidases 1Introduction 1Techniques and Instrumentation 2Summary and Conclusions 5References 62 Heme Peroxidase and Catalase Families 9Plant, Fungal, and Bacterial Peroxidases 9Mammalian Peroxidases 11Catalases 12References 123 Horseradish Peroxidase. I. The Native Enzyme, Compounds I and II, Their Structures, and Their Cycle 13Introduction 13The Classic Peroxidase Cycle 13Structure and Properties of Native Horseradish Peroxidase C 18Horseradish Peroxidase Compound I (HRP-I) 23Horseradish Peroxidase Compound II (HRP-II) 26Some Diverse Approaches to an Understanding of Horseradish Peroxidase 27References 304 Horseradish Peroxidase. II. Two-Electron Reactions, Ferrous Peroxidase, Compound III, The Five Oxidation States, Oxygen Evolution, and Inactivation 41Introduction 41Two-Electron Oxidations By Compound I 41Oxygen Transfer By One-Electron Mechanisms 44Ferrous Horseradish Peroxidase and Compound III 45The Five Oxidation States of Horseradish Peroxidase 48The Catalatic Reaction 50The HRP Clock Reaction 51Enzyme Inactivation 51References 525 Horseradish Peroxidase. III. Oscillations and Peroxidase-Oxidase Reactions with NADH, Indole-3- Acetic Acid, and Isobutyraldehyde. Light Emission 57Oscillations and the NADH Peroxidase-Oxidase Reaction 57Peroxidase Oxidase Reaction with Indole-3-Acetic Acid 63Reaction of Isobutyraldehyde with Horseradish Peroxidase 68References 706 Yeast Cytochrome c Peroxidase: Reactions with Small Substrates 77Introduction 77Properties of Yeast Cytochrome c Peroxidase 77Crystal Structures of Yeast Cytochrome c Peroxidase, its Compounds and Complexes 78Mechanism of Compound I Formation 80The Reaction Cycle for Yeast Cytochrome c Peroxidase 82Steady-State Kinetics 83References 917 Yeast Cytochrome c Peroxidase: Reaction with Cytochrome c 97Introduction 97Experimental Results 97References 1038 Spectroscopy. I. Optical, Resonance Raman, and X-Ray Absorption 107Optical Absorption Spectra 107Resonance Raman Spectra 111X-ray Absorption Spectroscopy 121References 1239 Spectroscopy. II. Nuclear Magnetic Resonance, Electron Spin, and MöSsbauer 129Nuclear Magnetic Resonance (NMR) Spectroscopy 129Electron Spin Resonance (ESR) Spectroscopy 139Mössbauer Spectroscopy 145References 14610 Theoretical 153Peroxidase Kinetics 153Marcus Theory for Electron Transfer Reactions 156Electron Tunneling 159Electron Transfer Reactions in Proteins 160Electron Density Circuits 161Diffusion Control 163Quantum Mechanical Calculations 164References 17111 Class I: Ascorbate Peroxidase 179Introduction 179Sequencing and Cloning 180Properties, Reactions, and Intermediate Compounds 181Crystal Structures 184References 18512 Catalase-Peroxidases and Mycobacterium Tuberculosis 189Introduction 189Structures of Catalase-Peroxidases 190Isoniazid and Other Reactants of Catalase-Peroxidases 192The Oxidative Defense Mechanisms of Mycobacterium Tuberculosis 196References 19613 Class II. Lignin, Manganese, Versatile, and Coprinus Cinereus Peroxidases 203Lignin Peroxidase 203Manganese Peroxidase 208Other Manganese Peroxidases, Versatile Peroxidase 210Coprinus Cinereus (Arthromyces Ramosus) Peroxidase 210References 21214 Other Class III Peroxidases 221Arabidopsis Thaliana Peroxidase 221Barley Peroxidase 222Peanut Peroxidase 223Soybean Peroxidase 225Tobacco Peroxidases 225Turnip Peroxidases 226References 22715 Catalases 233Peter JonesIntroduction 233Perspective 234Progress 235Catalases in Biology 248Prospects 250References 25216 Myeloperoxidase: Enzymology 257Introduction 257Properties of Myeloperoxidase 258The Compounds of Myeloperoxidase 260Reactions of Myeloperoxidase 264Cloning of Myeloperoxidase: Site-Directed Mutagenesis 266The Crystal Structure and the Prosthetic Group of Myeloperoxidase 266Eosinophil Peroxidase 268References 26917 Biomedical Aspects of Myeloperoxidase: Halogenation Reactions In Cardiovascular Disease, Infection, And Cancer 281Jeffrey P. Henderson and Jay. W. HeineckeIntroduction 281Oxidants Produced by MPO in Humans 281MPO and Coronary Artery Disease 286MPO and Carcinogenesis 288Prospects 290References 29018 Prostaglandin H Synthase 297Introduction 297Crystal Structures 299Prostaglandin H Synthase-2 300Preliminary Mechanistic Studies 302Detection of Free Radicals: Role of ESR Spectroscopy 303The Role of Aspirin and Related Substances: Contributions of Vane and Smith 304Work of Marnett and Coworkers 305Work of Kulmacz, Tsai, and Coworkers 305Manganese Prostaglandin Synthases 306Mechanistic Details 307References 31419 Thyroid Peroxidase 323Introduction 323Hormone Discovery and Chemical Synthesis 324Detection of the Method of Biological Synthesis of Thyroxine 325Conclusions 329References 32920 Lacto- And Salivary Peroxidases 335Introduction 335Properties 335The Compounds of Lactoperoxidase and Their Reactions 336References 33921 Chloroperoxidase From C. Fumago 345Introduction 345History 345Optical Spectra 347ESR, Endor, Mössbauer, Exafs, and Resonance Raman Spectra 348Investigations of Compounds I and II 348Structure of Compound I and the Catalatic Reaction 349Ligand Binding 350Kinetics and Mechanisms of Chlorination and Oxidation 351Amino Acid Sequence and Crystal Structure 353References 35322 Selenium-Containing Enzymes: Glutathione Peroxidase and Iodothyronine Deiodinase 359Introduction 359Glutathione Peroxidase 359Iodothyronine Deiodinase 361References 36123 Structure and Function of Vanadium Haloperoxidases 363Ron Wever and Rokus RenirieSummary 363Abbreviations 364Introduction 364Occurrence and Biological Function of Vanadium Iodo- and Bromoperoxidases 365Occurrence and Biological Function of Vanadium Chloroperoxidases 366Catalytic Properties of Bromoperoxidase 367Properties of the Prosthetic Group in Bromoperoxidase 370Kinetic and Optical Properties of Vanadium Chloroperoxidases 371Sulfoxidation Reactions 373Stability of Bromo- and Chloroperoxidases 374X-ray Structures of Vanadium Bromoperoxidases 374Active Site of Vanadium Bromoperoxidase From A. Nodosum 375X-ray Structures of the Vanadium Chloroperoxidase and Details of the Active Site 376X-ray Structure of the Peroxo-Intermediate of Vanadium Chloroperoxidase and Difference in Reactivity Between Chloro- and Bromoperoxidases 378Nature of the Vanadate Cofactor 380References 38224 Other Heme Peroxidases and Enzymes 387DI-Heme Peroxidases 387Peroxidases Everywhere You Look 389Myoglobins 391Hemoglobin 392Cytochrome c Oxidase 392Oxygenases 392Heme Oxygenase 394Guanylyl Cyclase 394References 39525 Application of Peroxidases 403Ron WeverIntroduction 403Background Information 403Peroxidases as Pharmaceutical and/or Antimicrobial Agents 404Applications in Bleaching and Detergents 411Biotransformations 412Polymerization Reactions and Wastewater Purification 414Depolymerization Reactions 415Analytical Applications 416Medical Applications 417References 417Author Index 425Subject Index 451