The second of two relatively independent volumes on the chemistry and biology of peroxidases. Volumes 2 covers the peroxidases isolated from plants and microorganisms, and includes detailed discussions of some of the unique reactions catalyzed by these enzymes. Volume one covered the peroxidases isolated from animal sources, as well as the "pseudo- peroxidase activity" of prostaglandin H synthase and of myoglobin and hemoglobin. Acidic paper. Annotation copyrighted by Book News, Inc., Portland, OR

SINGLE SOURCE GUIDE TO PEROXIDASES AND CATALASES Reflecting the important historical discoveries and exciting research in the field in recent years, Peroxidases and Catalases: Biochemistry, Biophysics, Biotechnology and Physiology provides a much-needed systematic, up-to-date treatment of peroxidases and catalases. From the structure and properties of the various superfamilies to current applications of peroxidases, the book 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. Considering the subject from both theoretical and applied perspectives, Peroxidases and Catalases offers a critical review of the literature and detailed discussions of the most current research. Chapters cover: The background and history of peroxidases and catalases Plant, fungal, and bacterial peroxidase superfamilies and their organization Mammalian peroxidases including medical and physiological roles Spectroscopic and theoretical techniques for studying peroxidases highlighting the contributions of physicists and physical/theoretical chemists Heme peroxidases, catalases, and other peroxidases such as vanadium and selenium peroxidase Relevant plant and animal physiology This one-stop reference is a vital reference for biochemists, biologists, biochemical engineers, physiologists, environmental and pharmaceutical researchers, and others interested in the study and use of peroxidases and catalases.