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