Biological Inorganic Chemistry
by Bertini, Gray, Stiefel, Valentine
ISBN: 9781938787966 | Copyright 2007
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The long awaited text for 21st century courses in biological inorganic chemistry is now available. Organized and edited by Ivano Bertini, Harry Gray, Ed Stiefel, and Joan Valentine, with contributions from many other world leaders in the field, this all-new book is equally appropriate for graduate or senior undergraduate courses in bioinorganic chemistry. The book has been extensively class-tested at Princeton and UCLA, and it includes tutorials in biology and biochemistry and in inorganic chemistry to aid students of varying backgrounds. The main text is divided into two parts. Part A, _x001C_Overviews of Biological Inorganic Chemistry,_x001D_ sets forth the unifying principles of the field. A full course in bioinorganic chemistry could be based entirely on this overview section, which is a really a book within a book! Part B, _x001C_Metal-Ion Containing Biological Systems,_x001D_ describes specific classes of systems in detail. A special feature is the strong connection to the genomic revolution that has dramatically enhanced our ability to define the function of gene products in living organisms. Throughout the book, protein data bank codes are given for structures discussed in the text, and students are encouraged to learn to use the PDB in their courses and research. This exciting new book will be a must read for years to come for all students and researchers interested in the field of biological inorganic chemistry.
Published under the University Science Books imprint
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|---|---|
| Front Cover (pg. i) | |
| Contents in Brief (pg. vii) | |
| Detailed Contents (pg. ix) | |
| List of Contributors (pg. xix) | |
| Preface (pg. xxiii) | |
| Acknowledgments (pg. xxv) | |
| Chapter I Introduction and Text Overview (pg. 1) | |
| PART A Overviews of Biological Inorganic Chemistry (pg. 5) | |
| Chapter II Bioinorganic Chemistry and the Biogeochemical Cycles (pg. 7) | |
| II.1. Introduction (pg. 7) | |
| II.2. The Origin and Abundance of the Chemical Elements (pg. 8) | |
| II.3. The Carbon/Oxygen/Hydrogen Cycles (pg. 12) | |
| II.4. The Nitrogen Cycle (pg. 16) | |
| II.5. The Sulfur Cycle (pg. 20) | |
| II.6. The Interaction and Integration of the Cycles (pg. 24) | |
| II.7. Conclusions (pg. 29) | |
| Chapter III Metal Ions and Proteins: Binding, Stability, and Folding (pg. 31) | |
| III.1. Introduction (pg. 31) | |
| III.2. The Metal Cofactor (pg. 31) | |
| III.3. Protein Residues as Ligands for Metal Ions (pg. 33) | |
| III.4. Genome Browsing (pg. 37) | |
| III.5. Folding and Stability of Metalloproteins (pg. 37) | |
| III.6. Kinetic Control of Metal Ion Delivery (pg. 40) | |
| Chapter IV Special Cofactors and Metal Clusters (pg. 43) | |
| IV.1. Why Special Metal Cofactors? (pg. 43) | |
| IV.2. Types of Cofactors, Structural Features, and Occurrence (pg. 46) | |
| IV.3. Cofactor Biosynthesis (pg. 54) | |
| Chapter V Transport and Storage of Metal Ions in Biology (pg. 57) | |
| V.1. Introduction (pg. 57) | |
| V.2. Metal Ion Bioavailability (pg. 59) | |
| V.3. General Properties of Transport Systems (pg. 61) | |
| V.4. Iron Illustrates the Problems of Metal Ion Transport (pg. 66) | |
| V.5. Transport of Metal Ions Other Than Iron (pg. 70) | |
| V.6. Mechanisms of Metal Ion Storage and Resistance (pg. 71) | |
| V.7. Intracellular Metal Ion Transport and Trafficking (pg. 74) | |
| V.8. Summary (pg. 76) | |
| Chapter VI Biominerals and Biomineralization (pg. 79) | |
| VI.1. Introduction (pg. 79) | |
| VI.2. Biominerals: Types and Functions (pg. 79) | |
| VI.3. General Principles of Biomineralization (pg. 83) | |
| VI.4. Conclusions (pg. 93) | |
| Chapter VII Metals in Medicine (pg. 95) | |
| VII.1. Introduction (pg. 95) | |
| VII.2. Metallotherapeutics (pg. 96) | |
| VII.3. Imaging and Diagnosis (pg. 114) | |
| VII.4. Molecular Targets (pg. 122) | |
| VII.5. Metal Metabolism as a Therapeutic Target (pg. 129) | |
| VII.6. Conclusions (pg. 132) | |
| PART B Metal Ion Containing Biological Systems (pg. 137) | |
| Chapter VIII Metal Ion Transport and Storage (pg. 139) | |
| VIII.1. Transferrin (pg. 139) | |
| VIII.2. Ferritin (pg. 144) | |
| VIII.3. Siderophores (pg. 151) | |
| VIII.4. Metallothioneins (pg. 156) | |
| VIII.5. Copper-Transporting ATPases (pg. 163) | |
| VIII.6. Metallochaperones (pg. 166) | |
| Chapter IX Hydrolytic Chemistry (pg. 175) | |
| IX.1. Metal-Dependent Lyase and Hydrolase Enzymes. (I) General Metabolism (pg. 175) | |
| IX.2. Metal-Dependent Lyase and Hydrolase Enzymes. (II) Nucleic Acid Biochemistry (pg. 185) | |
| IX.3. Urease (pg. 198) | |
| IX.4. Aconitase (pg. 209) | |
| IX.5. Catalytic Nucleic Acids (pg. 215) | |
| Chapter X Electron Transfer, Respiration, and Photosynthesis (pg. 229) | |
| X.1. Electron-Transfer Proteins (pg. 229) | |
| X.2. Electron Transfer through Proteins (pg. 261) | |
| X.3. Photosynthesis and Respiration (pg. 278) | |
| X.4. Dioxygen Production: Photosystem II (pg. 302) | |
| Chapter XI Oxygen Metabolism (co-edited by Lawrence Que, Jr.) (pg. 319) | |
| XI.1. Dioxygen Reactivity and Toxicity (pg. 319) | |
| XI.2. Superoxide Dismutases and Reductases (pg. 331) | |
| XI.3. Peroxidase and Catalases (pg. 343) | |
| XI.4. Dioxygen Carriers (pg. 354) | |
| XI.5. Dioxygen Activating Enzymes (pg. 388) | |
| XI.6. Reducing Dioxygen to Water: Cytochrome c Oxidase (pg. 413) | |
| XI.7. Reducing Dioxygen to Water: Multi-Copper Oxidases (pg. 427) | |
| XI.8. Reducing Dioxygen to Water: Mechanistic Considerations (pg. 440) | |
| Chapter XII Hydrogen, Carbon, and Sulfur Metabolism (pg. 443) | |
| XII.1. Hydrogen Metabolism and Hydrogenase (pg. 443) | |
| XII.2. Metalloenzymes in the Reductionof One-Carbon Compounds (pg. 452) | |
| XII.3. Biological Nitrogen Fixation and Nitrification (pg. 468) | |
| XII.4. Nitrogen Metabolism: Denitrification (pg. 494) | |
| XII.5. Sulfur Metabolism (pg. 508) | |
| XII.6. Molybdenum Enzymes (pg. 518) | |
| XII.7. Tungsten Enzymes (pg. 545) | |
| Chapter XIII Metalloenzymes with Radical Intermediates (pg. 557) | |
| XIII.1. Introduction to Free Radicals (pg. 557) | |
| XIII.2. Cobalamins (pg. 562) | |
| XIII.3. Ribonucleotide Reductases (pg. 575) | |
| XIII.4. FeaS Clusters in Radical Generation (pg. 582) | |
| XIII.5. Galactose Oxidase (pg. 595) | |
| XIII.6. Amine Oxidases (pg. 601) | |
| XIII.7. Lipoxygenase (pg. 607) | |
| Chapter XIV Metal Ion Receptors and Signaling (pg. 613) | |
| XIV.1. Metalloregulatory Proteins (pg. 613) | |
| XIV.2. Structural Zinc-Binding Domains (pg. 628) | |
| XIV.3. Calcium in Mammalian Cells (pg. 635) | |
| XIV.4. Nitric Oxide (pg. 647) | |
| Cell Biology, Biochemistry, and Evolution: Tutorial I (pg. 657) | |
| T.I.1. Life’s Diversity (pg. 657) | |
| T.I.2. Evolutionary History (pg. 666) | |
| T.I.3. Genomes and Proteomes (pg. 668) | |
| T.I.4. Cellular Components (pg. 670) | |
| T.I.5. Metabolism (pg. 685) | |
| Fundamentals of Coordination Chemistry: Tutorial II (pg. 695) | |
| T.II.1. Introduction (pg. 695) | |
| T.II.2. Complexation Equilibria in Water (pg. 695) | |
| T.II.3. The Effect of Metal Ions on the pKa of Ligands (pg. 698) | |
| T.II.4. Ligand Specificity: Hard versus Soft (pg. 698) | |
| T.II.5. Coordination Chemistry and Ligand-Field Theory (pg. 700) | |
| T.II.6. Consequences of Ligand-Field Theory (pg. 703) | |
| T.II.7. Kinetic Aspects of Metal Ion Binding (pg. 708) | |
| T.II.8. Redox Potentials and Electron-Transfer Reactions (pg. 709) | |
| Appendix I Abbreviations (pg. 713) | |
| Appendix II Glossary (pg. 717) | |
| Appendix III The Literature of Biological Inorganic Chemistry (pg. 727) | |
| Appendix IV Introduction to the Protein Data Bank (PDB) (pg. 729) | |
| Index (pg. 731) | |
| Back Cover (pg. 740) | |
Harry B. Gray
Harry Barkus Gray is the Arnold O. Beckman Professor of Chemistry and the Founding Director of the Beckman Institute at the California Institute of Technology. His main research interests center on inorganic spectroscopy, photochemistry, and bioinorganic chemistry, with emphasis on understanding electron transfer in proteins. For his contributions to chemistry, which include over 700 papers and 17 books, he has received the National Medal of Science from President Ronald Reagan (1986); the Linderstrøm-Lang Prize (1991); the Basolo Medal (1994); the Gibbs Medal (1994); the Chandler Medal (1999); the Harvey Prize (2000); the Nichols Medal (2003); the National Academy of Sciences Award in Chemical Sciences (2003); the Benjamin Franklin Medal in Chemistry (2004); the Wolf Prize in Chemistry (2004); the City of Florence Prize in Molecular Sciences (2006); six national awards from the American Chemical Society, including the Priestley Medal (1991); and 16 honorary doctorates. He is a member of the National Academy of Sciences; the American Academy of Arts and Sciences; the American Philosophical Society; an honorary member of the Italian Chemical Society; a foreign member of the Royal Danish Academy of Sciences and Letters; the Royal Swedish Academy of Sciences; and the Royal Society of Great Britain. He was California Scientist of the Year in 1988.|
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