Dunford H.B. Peroxidases and catalases: biochemistry, biophysics, biotechnology, and physiology (Hoboken, 2010). - ОГЛАВЛЕНИЕ / CONTENTS
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ОбложкаDunford H.B. Peroxidases and catalases: biochemistry, biophysics, biotechnology, and physiology. - 2nd ed. - Hoboken: Wiley, 2010. - xv, 459 p.: ill. - Incl. bibl. ref. - Auth. ind.: p.425-449. - Sub. ind.: p.451-459. - ISBN 978-0-470-22476-2
 

Оглавление / Contents
 
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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