Heme Peroxidases

About this book

This book reflects the tremendous growth peroxidases research has experienced in recent years, providing for the first time in over three decades a systematic, up-to-date treatment of the subject. From cancer in plants to unique saddle-shaped hemes in peroxidases, it consolidates vast amounts of information previously scattered in the professional literature, covering all aspects of these ubiquitous enzymes that act on a variety of substances and processes in living systems-their properties, reactions, crystal structures, cloning, and more. Complete with hundreds of vivid illustrations, many in color or 3D, Heme Peroxidases presents Welinder's recent classification of the enzymes according to their evolutionary development; X-ray crystallographic data on many peroxidases; a step-by-step introduction to modern spectroscopic techniques used in peroxidases research; an appendix listing amino acid sequences for all enzymes and catalases described in the book; and over 1,700 references to current results. This one-stop reference for analytical biochemists, biotechnologists, and others interested in the study and use of peroxidases, offers a critical review of the literature, and sorts through the various conflicting reports about peroxidase mechanisms. It familiarizes the reader with commercial and industrial applications in analytical biochemistry, biotechnology, medicine, agriculture, and the environment - addressing future trends in drug synthesis, water purification, and soil decontamination.

Contents

Historical Background.; Model Peroxidases from Yeast and Horseradish, Cloned Enzymes, Comparison to Metmyoglobin.; Heme Peroxidase and Catalase Families and Superfamilies: Crystal Structures.; Horseradish Peroxidase I: Ligand Binding, Redox Potentials, Formation of Its Compounds, and Some of Their Reactions.; Horseradish Peroxidase II: Isoenzymes, Steady State Kinetics, and Peroxidase--Oxidase Reaction.; Horseradish Peroxidase III: Reaction with Indole--3--Acetic Acid, Light Emission, Quantitative Structure--Activity Relationships.; Spectroscopy of Horseradish Peroxidase I: Optical, Resonance Raman, Magnetic Circular Dichroism, X--ray Absorption, and Diffraction.; Spectroscopy of Horeradish Peroxidase II: Nuclear Magnetic Resonance, Electron Paramagnetic Resonance, Electron Nuclear Double Resonance, Mossbauer Spectroscopy, and Theoretical Studies.; Yeast Cytochrome c Peroxidase I: Properties and Reactions with Small Molecules.; Yeast Cytochrome c Peroxidase II: Interaction with Cytochrome c.; Other Class I Peroxidases: Ascorbate Peroxidase and Bacterial Catalase--Peroxidases.; Class II Peroxidases: Lignin, Manganese, and Coprinus cinereus Peroxidases.; Other Class III Plant Peroxidases: Peanuts, Barley, Tobacco, and Arabidopsis thaliana.; Chloroperoxidase and Pseudomonas Cytochrome c Peroxidase.; Myeloperoxidase and Eosinophil Peroxidase: Phagocytosis and Microbial Killing.; Prostaglandin Endoperoxide H Synthases.; Lactoperoxidase, Thyroid Peroxidase, and Other Animal Peroxidases.; Catalases.; Appendix.; Index.

Customer Reviews

Biography

H. BRIAN DUNFORD is Professor of Biophysical Chemistry and formerly Associate Dean of Research for the Faculty of Science at the University of Alberta where he has been teaching for three decades.