PREFACE ...................................................... XIII
CONTRIBUTORS ................................................... XV
1 HISTORICAL: PIONEERING WORK ON HORSERADISH AND YEAST
CYTOCHROME с 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 С ................................................ 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 1 ....................... 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 с PEROXIDASE: REACTIONS WITH SMALL
SUBSTRATES .................................................. 77
Introduction ................................................ 77
Properties of Yeast Cytochrome с Peroxidase ................. 77
Crystal Structures of Yeast Cytochrome с Peroxidase, its
Compounds and Complexes ..................................... 78
Mechanism of Compound I Formation ........................... 80
The Reaction Cycle for Yeast Cytochrome с Peroxidase ........ 82
Steady-State Kinetics ....................................... 83
References .................................................. 91
7 YEAST CYTOCHROME с PEROXIDASE: REACTION WITH CYTOCHROME ..... 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
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
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
Arabidopsis Thaliana Peroxidase ............................ 221
Barley Peroxidase .......................................... 222
Peanut Peroxidase .......................................... 223
Soybean Peroxidase ......................................... 225
Tobacco Peroxidases ........................................ 225
Turnip Peroxidases ......................................... 226
References ................................................. 227
15 CATALASES
Peter Jones
Introduction ............................................... 233
Perspective ................................................ 234
Progress ................................................... 235
Catalases in Biology ....................................... 248
Prospects .................................................. 250
References ................................................. 252
16 MYELOPEROXIDASE: ENZYMOLOGY
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 С. FUMAGO ............................ 345
Introduction ............................................... 345
History .................................................... 345
Optical Spectra ............................................ 347
ESR, Endor, Mössbauer, Exafs, and Resonance Raman
Spectra .................................................... 348
Investigations of Compounds I and П ........................ 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
DI-Heme Peroxidases ........................................ 387
Peroxidases Everywhere You Look ............................ 389
Myoglobins ................................................. 391
Hemoglobin ................................................. 392
Cytochrome с Oxidase ....................................... 392
Oxygenases ................................................. 392
Heme Oxygenase ............................................. 394
Guanylyl Cyclase ........................................... 394
References ................................................. 395
25 APPLICATION OF PEROXIDASES
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
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