Peroxidases and Catalases
Biochemistry, Biophysics, Biotechnology and Physiology
2. Edition March 2010
480 Pages, Hardcover
Wiley & Sons Ltd
ISBN:
978-0-470-22476-2
John Wiley & Sons
Short 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.
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.
Preface.
1 Historical Pioneering work on horseradish and yeast cytochrome c peroxidases.
Introduction.
Techniques and instrumentation.
Conclusions.
2 Heme peroxidase and catalase families.
Plant, fungal and bacterial peroxidases.
Mammalian peroxidases.
Catalases.
3 Horseradish peroxidase I. The native enzyme, Compounds I and 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 horseradish peroxidase.
4 Horseradish peroxidase II. Two-electron reactions, ferrous peroxidase, Compound III, the five oxidation states, oxygen evolution, 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.
5 Horseradish peroxidase III. Oscillations and peroxidase-oxidase reactions with NADH, indole-3-acetic acid and isobutyraldehyde.
Oscillations and the NADH peroxidase-oxidase reaction.
Peroxidase-oxidase reaction with indole-3-acetic acid.
Reaction of isobutyraldehyde with horseradish peroxidase.
6 Yeast cytochrome c peroxidase. Reactions with small substrates.
Introduction.
Properties of yeast cytochrome c peroxidase.
Crystal structures of yeast cytochrome c peroxidase, its compounds and complexes.
Mechanism of Compound I formation.
The reaction cycle for yeast cytochrome c peroxidase.
Steady state kinetics.
7 Yeast cytochrome c peroxidase. Reaction with cytochrome c.
Introduction.
Experimental results.
8 Spectroscopy I. Optical, resonance Raman, and X-ray absorption.
Optical absorption spectroscopy.
Resonance Raman spectra.
X-ray absorption spectroscopy.
9 Spectroscopy II. Nuclear magnetic resonance, electron spin, and M"ssbauer.
Nuclear magnetic resonance (NMR) spectroscopy.
Electron spin resonance (ESR) spectroscopy.
M"ssbauer spectroscopy.
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.
11 Class I: ascorbate peroxidase.
Ascorbate peroxidase.
12 Catalase-peroxidases and Mycobacterium tuberculosis.
Introduction.
Structures of catalase-peroxidases.
Isoniazid and other reactants of catalase-peroxidases.
The oxidative defence mechanisms of Mycobacterium tuberculosis.
13 Class II. Lignin, manganese, versatile, and Coprinus cinereus peroxidases.
Lignin peroxidase.
Manganese peroxidase.
Other manganese peroxidases, versatile peroxidase.
Coprinus cinereus (Arthromyces ramosus) peroxidase.
14 Other Class III peroxidases.
Arabidopsis thaliana peroxidase.
Barley peroxidase.
Peanut peroxidase.
Soybean peroxidase.
Tobacco peroxidases.
Turnip peroxidases.
15 Catalases.
Preamble.
Perspective.
Progress.
Catalases in biology.
Prospects.
16 Myeloperoxidase. Enzymology.
Introduction.
Properties of myeloperoxidase.
The compounds of myeloperoxidase.
Reactions of myeloperoxidase.
Cloning of myeloperoxidase. Site-directed mutagenesis.
The crystal structure and prosthetic group of myeloperoxidase.
Eosinophil peroxidase.
17 Biomedical aspects of myeloperoxidase. Halogenation reactions in cardiovascular disease, infection and cancer.
Introduction.
Oxidants produced by MPO in humans.
MPO and coronary artery disease.
MPO and carcinogenesis.
Prospects.
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 of Vane and Smith.
Work of Marnett and coworkers.
Work of Kulmacz, Tsai and coworkers.
Manganese prostaglandin synthases.
Mechanistic details.
19 Thyroid peroxidase.
Introduction.
Hormone discovery and chemical synthesis.
Detection of the method of biological synthesis of thyroxine.
Conclusions.
20 Lacto- and salivary peroxidases.
Introduction.
The compounds of lactoperoxidase and their reactions.
21 Heme chloroperoxidase from C. fumago.
Introduction.
Optical spectra.
ESR, ENDOR, M"ssbauer, EXAFS and resonance Raman spectra.
Structure of Compound I and the catalatic reaction.
Ligand binding.
Kinetics and mechanism of chlorination and oxidation.
Amino acid sequence and crystal structure.
22 Selenium-containing enzymes: glutathione peroxidase and iodothyronine deiodinase.
Introduction.
Glutathione peroxidase.
Iodothyronine deiodinase.
23 Structure and function of vanadium peroxidases.
Summary.
Introduction.
Occurrence and biological function of vanadium iodo- and bromoperoxidases.
Catalytic properties of BPO.
Properties of the prosthetic group in bromoperoxidase.
Kinetic and optical properties of vanadium chloroperoxidases.
Sulfoxidation reactions.
Stability of bromo- and chloroperoxidases.
X-ray structures of vanadium bromoperoxidases.
Active site of vanadium bromoperoxidase from A. nodsum.
X-ray structure of the peroxy-intermediate of vanadium chloroperoxidase.
Nature of the vanadate cofactor.
24 Other heme peroxidases and enzymes.
Di-heme peroxidases.
Peroxidases everywhere you look.
Myoglobins.
Hemoglobin.
Cytochrome c oxidase.
Oxygenases.
Heme oxygenase.
Guanylyl cyclase.
25 Application of peroxidases.
Introduction.
Background information.
Peroxidases as pharmaceutical and/or antimicrobial agents.
Applications in bleaching and detergents.
Biotransformations.
Polymerization reactions and waste water purification.
Depolymerization reactions.
Analytical applications.
Medical applications.
1 Historical Pioneering work on horseradish and yeast cytochrome c peroxidases.
Introduction.
Techniques and instrumentation.
Conclusions.
2 Heme peroxidase and catalase families.
Plant, fungal and bacterial peroxidases.
Mammalian peroxidases.
Catalases.
3 Horseradish peroxidase I. The native enzyme, Compounds I and 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 horseradish peroxidase.
4 Horseradish peroxidase II. Two-electron reactions, ferrous peroxidase, Compound III, the five oxidation states, oxygen evolution, 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.
5 Horseradish peroxidase III. Oscillations and peroxidase-oxidase reactions with NADH, indole-3-acetic acid and isobutyraldehyde.
Oscillations and the NADH peroxidase-oxidase reaction.
Peroxidase-oxidase reaction with indole-3-acetic acid.
Reaction of isobutyraldehyde with horseradish peroxidase.
6 Yeast cytochrome c peroxidase. Reactions with small substrates.
Introduction.
Properties of yeast cytochrome c peroxidase.
Crystal structures of yeast cytochrome c peroxidase, its compounds and complexes.
Mechanism of Compound I formation.
The reaction cycle for yeast cytochrome c peroxidase.
Steady state kinetics.
7 Yeast cytochrome c peroxidase. Reaction with cytochrome c.
Introduction.
Experimental results.
8 Spectroscopy I. Optical, resonance Raman, and X-ray absorption.
Optical absorption spectroscopy.
Resonance Raman spectra.
X-ray absorption spectroscopy.
9 Spectroscopy II. Nuclear magnetic resonance, electron spin, and M"ssbauer.
Nuclear magnetic resonance (NMR) spectroscopy.
Electron spin resonance (ESR) spectroscopy.
M"ssbauer spectroscopy.
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.
11 Class I: ascorbate peroxidase.
Ascorbate peroxidase.
12 Catalase-peroxidases and Mycobacterium tuberculosis.
Introduction.
Structures of catalase-peroxidases.
Isoniazid and other reactants of catalase-peroxidases.
The oxidative defence mechanisms of Mycobacterium tuberculosis.
13 Class II. Lignin, manganese, versatile, and Coprinus cinereus peroxidases.
Lignin peroxidase.
Manganese peroxidase.
Other manganese peroxidases, versatile peroxidase.
Coprinus cinereus (Arthromyces ramosus) peroxidase.
14 Other Class III peroxidases.
Arabidopsis thaliana peroxidase.
Barley peroxidase.
Peanut peroxidase.
Soybean peroxidase.
Tobacco peroxidases.
Turnip peroxidases.
15 Catalases.
Preamble.
Perspective.
Progress.
Catalases in biology.
Prospects.
16 Myeloperoxidase. Enzymology.
Introduction.
Properties of myeloperoxidase.
The compounds of myeloperoxidase.
Reactions of myeloperoxidase.
Cloning of myeloperoxidase. Site-directed mutagenesis.
The crystal structure and prosthetic group of myeloperoxidase.
Eosinophil peroxidase.
17 Biomedical aspects of myeloperoxidase. Halogenation reactions in cardiovascular disease, infection and cancer.
Introduction.
Oxidants produced by MPO in humans.
MPO and coronary artery disease.
MPO and carcinogenesis.
Prospects.
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 of Vane and Smith.
Work of Marnett and coworkers.
Work of Kulmacz, Tsai and coworkers.
Manganese prostaglandin synthases.
Mechanistic details.
19 Thyroid peroxidase.
Introduction.
Hormone discovery and chemical synthesis.
Detection of the method of biological synthesis of thyroxine.
Conclusions.
20 Lacto- and salivary peroxidases.
Introduction.
The compounds of lactoperoxidase and their reactions.
21 Heme chloroperoxidase from C. fumago.
Introduction.
Optical spectra.
ESR, ENDOR, M"ssbauer, EXAFS and resonance Raman spectra.
Structure of Compound I and the catalatic reaction.
Ligand binding.
Kinetics and mechanism of chlorination and oxidation.
Amino acid sequence and crystal structure.
22 Selenium-containing enzymes: glutathione peroxidase and iodothyronine deiodinase.
Introduction.
Glutathione peroxidase.
Iodothyronine deiodinase.
23 Structure and function of vanadium peroxidases.
Summary.
Introduction.
Occurrence and biological function of vanadium iodo- and bromoperoxidases.
Catalytic properties of BPO.
Properties of the prosthetic group in bromoperoxidase.
Kinetic and optical properties of vanadium chloroperoxidases.
Sulfoxidation reactions.
Stability of bromo- and chloroperoxidases.
X-ray structures of vanadium bromoperoxidases.
Active site of vanadium bromoperoxidase from A. nodsum.
X-ray structure of the peroxy-intermediate of vanadium chloroperoxidase.
Nature of the vanadate cofactor.
24 Other heme peroxidases and enzymes.
Di-heme peroxidases.
Peroxidases everywhere you look.
Myoglobins.
Hemoglobin.
Cytochrome c oxidase.
Oxygenases.
Heme oxygenase.
Guanylyl cyclase.
25 Application of peroxidases.
Introduction.
Background information.
Peroxidases as pharmaceutical and/or antimicrobial agents.
Applications in bleaching and detergents.
Biotransformations.
Polymerization reactions and waste water purification.
Depolymerization reactions.
Analytical applications.
Medical applications.
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.
