Main description:

Peroxidases and Catalases provides a summary of current research on peroxidase and catalase enzymes, along with detailed chapters on mammalian peroxidases, medical and physiological roles, as well as spectroscopic and theoretical techniques, enabling biochemists to understand the contributions made principally by physicists and physical/theoretical chemists. Plus, the text discusses heme peroxidases and catalases, as well as other peroxidases, like vanadium peroxidases and selenium peroxidase. This book is a vital reference on peroxidases and catalases for engineers and researchers.

Contents:

PREFACE. CONTRIBUTORS. 1 HISTORICAL: PIONEERING WORK ON HORSERADISH AND YEASTCYTOCHROME c PEROXIDASES. Introduction. Techniques and Instrumentation. Summary and Conclusions. References. 2 HEME PEROXIDASE AND CATALASE FAMILIES. Plant, Fungal, and Bacterial Peroxidases. Mammalian Peroxidases. Catalases. References. 3 HORSERADISH PEROXIDASE. I. THE NATIVE ENZYME, COMPOUNDS IAND II, THEIR STRUCTURES, AND THEIR CYCLE. Introduction. The Classic Peroxidase Cycle. Structure and Properties of Native Horseradish Peroxidase C. Horseradish Peroxidase Compound I (HRP-I). Horseradish Peroxidase Compound II (HRP-II). Some Diverse Approaches to an Understanding of HorseradishPeroxidase. References. 4 HORSERADISH PEROXIDASE. II. TWO-ELECTRON REACTIONS, FERROUSPEROXIDASE, COMPOUND III, THE FIVE OXIDATION STATES, OXYGENEVOLUTION, AND INACTIVATION. Introduction. Two-Electron Oxidations By Compound I. Oxygen Transfer By One-Electron Mechanisms. Ferrous Horseradish Peroxidase and Compound III. The Five Oxidation States of Horseradish Peroxidase. The Catalatic Reaction. The HRP Clock Reaction. Enzyme Inactivation. References. 5 HORSERADISH PEROXIDASE. III. OSCILLATIONS ANDPEROXIDASE-OXIDASE REACTIONS WITH NADH, INDOLE-3-ACETIC ACID, ANDISOBUTYRALDEHYDE. LIGHT EMISSION. Oscillations and the NADH Peroxidase-Oxidase Reaction. Peroxidase Oxidase Reaction with Indole-3-Acetic Acid. Reaction of Isobutyraldehyde with Horseradish Peroxidase. References. 6 YEAST CYTOCHROME c PEROXIDASE: REACTIONS WITH SMALLSUBSTRATES. Introduction. Properties of Yeast Cytochrome c Peroxidase. Crystal Structures of Yeast Cytochrome c Peroxidase, itsCompounds and Complexes. Mechanism of Compound I Formation. The Reaction Cycle for Yeast Cytochrome c Peroxidase. Steady-State Kinetics. References . 7 YEAST CYTOCHROME c PEROXIDASE: REACTION WITHCYTOCHROME c. Introduction. Experimental Results. References. 8 SPECTROSCOPY. I. OPTICAL, RESONANCE RAMAN, AND X-RAYABSORPTION. Optical Absorption Spectra. Resonance Raman Spectra. X-ray Absorption Spectroscopy. References. 9 SPECTROSCOPY. II. NUCLEAR MAGNETIC RESONANCE, ELECTRONSPIN, AND MOSSBAUER. Nuclear Magnetic Resonance (NMR) Spectroscopy. Electron Spin Resonance (ESR) Spectroscopy. Mossbauer Spectroscopy. References. 10 THEORETICAL. Peroxidase Kinetics. Marcus Theory for Electron Transfer Reactions. Electron Tunneling. Electron Transfer Reactions in Proteins. Electron Density Circuits. Diffusion Control. Quantum Mechanical Calculations. References. 11 CLASS I: ASCORBATE PEROXIDASE. Introduction. Sequencing and Cloning. Properties, Reactions, and Intermediate Compounds. Crystal Structures. References. 12 CATALASE-PEROXIDASES AND MYCOBACTERIUMTUBERCULOSIS. Introduction. Structures of Catalase-Peroxidases. Isoniazid and Other Reactants of Catalase-Peroxidases. The Oxidative Defense Mechanisms of MycobacteriumTuberculosis. References. 13 CLASS II. LIGNIN, MANGANESE, VERSATILE, AND COPRINUSCINEREUS PEROXIDASES. Lignin Peroxidase. Manganese Peroxidase. Other Manganese Peroxidases, Versatile Peroxidase. Coprinus Cinereus (Arthromyces Ramosus) Peroxidase. References. 14 OTHER CLASS III PEROXIDASES. Arabidopsis Thaliana Peroxidase. Barley Peroxidase. Peanut Peroxidase. Soybean Peroxidase. Tobacco Peroxidases. Turnip Peroxidases. References. 15 CATALASES (Peter Jones). Introduction. Perspective. Progress. Catalases in Biology. Prospects. References. 16 MYELOPEROXIDASE: ENZYMOLOGY. Introduction. Properties of Myeloperoxidase. The Compounds of Myeloperoxidase. Reactions of Myeloperoxidase. Cloning of Myeloperoxidase: Site-Directed Mutagenesis. The Crystal Structure and the Prosthetic Group ofMyeloperoxidase. Eosinophil Peroxidase. References. 17 BIOMEDICAL ASPECTS OF MYELOPEROXIDASE: HALOGENATIONREACTIONS IN CARDIOVASCULAR DISEASE, INFECTION, AND CANCER(Jeffrey P. Henderson and Jay. W. Heinecke). Introduction. Oxidants Produced by MPO in Humans. MPO and Coronary Artery Disease. MPO and Carcinogenesis. Prospects. References. 18 PROSTAGLANDIN H SYNTHASE. Introduction. Crystal Structures. Prostaglandin H Synthase-2. Preliminary Mechanistic Studies. Detection of Free Radicals: Role of ESR Spectroscopy. The Role of Aspirin and Related Substances: Contributions ofVane and Smith. Work of Marnett and Coworkers. Work of Kulmacz, Tsai, and Coworkers. Manganese Prostaglandin Synthases. Mechanistic Details. References. 19 THYROID PEROXIDASE. Introduction. Hormone Discovery and Chemical Synthesis. Detection of the Method of Biological Synthesis ofThyroxine. Conclusions. References. 20 LACTO- AND SALIVARY PEROXIDASES. Introduction. Properties. The Compounds of Lactoperoxidase and Their Reactions. References. 21 CHLOROPEROXIDASE FROM C. FUMAGO. Introduction. History. Optical Spectra. ESR, Endor, Mossbauer, Exafs, and Resonance RamanSpectra. Investigations of Compounds I and II. Structure of Compound I and the Catalatic Reaction. Ligand Binding. Kinetics and Mechanisms of Chlorination and Oxidation. Amino Acid Sequence and Crystal Structure. References. 22 SELENIUM-CONTAINING ENZYMES: GLUTATHIONE PEROXIDASE ANDIODOTHYRONINE DEIODINASE. Introduction. Glutathione Peroxidase. Iodothyronine Deiodinase. References. 23 STRUCTURE AND FUNCTION OF VANADIUM HALOPEROXIDASES(Ron Wever and Rokus Renirie). Summary. Abbreviations. Introduction. Occurrence and Biological Function of Vanadium Iodo- andBromoperoxidases. Occurrence and Biological Function of VanadiumChloroperoxidases. Catalytic Properties of Bromoperoxidase. Properties of the Prosthetic Group in Bromoperoxidase. Kinetic and Optical Properties of VanadiumChloroperoxidases. Sulfoxidation Reactions. Stability of Bromo- and Chloroperoxidases. X-ray Structures of Vanadium Bromoperoxidases. Active Site of Vanadium Bromoperoxidase From A.Nodosum. X-ray Structures of the Vanadium Chloroperoxidase and Details ofthe Active Site. X-ray Structure of the Peroxo-Intermediate of VanadiumChloroperoxidase and Difference in Reactivity Between Chloro- andBromoperoxidases. Nature of the Vanadate Cofactor. References. 24 OTHER HEME PEROXIDASES AND ENZYMES. DI-Heme Peroxidases. Peroxidases Everywhere You Look. Myoglobins. Hemoglobin. Cytochrome c Oxidase. Oxygenases. Heme Oxygenase. Guanylyl Cyclase. References. 25 APPLICATION OF PEROXIDASES (Ron Wever). Introduction. Background Information. Peroxidases as Pharmaceutical and/or Antimicrobial Agents. Applications in Bleaching and Detergents. Biotransformations. Polymerization Reactions and Wastewater Purification. Depolymerization Reactions. Analytical Applications. Medical Applications. References. AUTHOR INDEX. SUBJECT INDEX.