Metalloproteins: Part 1: Metal Proteins with Redox Roles (Hardback)Pauline M. Harrison (editor)
Hardback Published: 31/12/1985
- Not available
The essays collected here seek to arrive at an understanding of how metalloprotein molecules work and the relationship of their functions to their own structures and to the functions and structures of other biomolecules. Part one encompasses both molecules for which three-dimensional structures are already available and complexes for which structural information is lacking or incomplete. It deals primarily with transition metals. Part two brings together six classes of protein to illustrate a variety of important physiological processes in which metals are involved in association with protein. The illustrated processes are divided into two types: those in which the metal center is required for a specific biological activity, and those in which the metal is being transported or sequestered and the proteins concerned control the provision of the metal in the right place at the right time in the correct amount. The three activities illustrated are enzyme catalysis, triggering, and oxygen transport. The essays reflect the current state of scientific knowledge, and will be of interest to biochemists, bioinorganic chemists, physiologists, molecular biologists, and enzymologists. ''The modest size of this book does not reflect the wealth of information it contains, most of which has been obtained in recent years. Each of the selected accounts represents important progress in modern inorganic biochemistry, progress that would be unthinkable without the successful cross-fertilization of several disciplines, such as physicochemistry, structural protein chemistry, and biochemistry...This book should be most valuable to the advanced student and researcher in the chemical and biomedical sciences...the editor can be congratulated for assembling a very valuable synopsis of current progress and understanding in this field...'' -- QUARTERLY REVIEW OF BIOLOGY
Publisher: Wiley-VCH Verlag GmbH
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