Note: Cover -- Half Title -- Title Page -- Copyright Page -- Contents -- PREFACE -- CONTRIBUTORS -- HANDBOOK ON TOXICITY OF INORGANIC COMPOUNDS -- HANDBOOK ON METALS IN CLINICAL AND ANALYTICAL CHEMISTRY -- METAL IONS IN BIOLOGICAL SYSTEMS (list of volumes) -- COLOR FIGURES -- Chapter 1 SCOPE AND USE OF THE HANDBOOK -- 1. Scope of the Handbook -- 2. Organization of the Handbook -- 3. Some Web Sites for Further Information -- 4. General Comments and Outlook -- References -- Chapter 2 INTERACTION OF SODIUM AND POTASSIUM WITH PROTEINS -- 1. Introduction -- 1.1. Bioinorganic Chemistry of Na+ and K+ -- 1.2. Coordination Chemistry of Na+ and K+ -- 2. Enzymes/Proteins with Known Structure -- 3. Enzymes/Proteins with Unknown Structure -- 4. Structure-Function Relationships -- 4.1. Dialkylglycine Decarboxylase -- 4.2. Pyruvate Kinase -- 4.3. Diol Dehydratase -- 4.4. Hsc70 -- 4.5. Class II Fructose-1,6-Bisphosphate Aldolase -- 4.6. Fructose-1,6-Bisphosphatase -- 4.7. Carbamoyl Phosphate Synthetase -- 4.8. Cytochrome P450cam -- 4.9. S-Adenosylmethionine Synthetase -- 4.10. Tryptophan Synthase a2p2 Complex -- 4.11. Tryptophanase -- 4.12. Tyrosine Phenol-Lyase -- 4.13. Ascorbate Peroxidase -- 4.14. Methionine Aminopeptidase -- 4.15. Thrombin -- 4.16. a-Amylase -- 5. Perspectives -- Acknowledgments -- Abbreviations and Definitions -- References -- Chapter 3 STRUCTURE AND FUNCTION OF SODIUM AND POTASSIUM CHANNEL PROTEINS IN MEMBRANES -- 1. Introduction -- 1.1. Ion Channels: Definition and Role in Excitable Membranes -- 1.2. How Do Voltage-Gated Ion Channels Work? -- 2. Potassium and Sodium Channel Proteins with Known Primary Structure -- 2.1. Potassium Channels -- 2.2. Sodium Channels -- 3. Structures of Channel Proteins and Protein Domains Resolved to Date -- 3.1. The Pore of a Bacterial Potassium Channel. , 3.2. Inactivation Domains of Mammalian Potassium and Sodium Channels -- 4. Structure-Function Relationships -- 4.1. Selectivity and Permeation -- 4.2. Gating: Activation and Inactivation -- 5. Perspectives -- Acknowledgments -- Abbreviations and Definitions -- References -- Chapter 4 MAGNESIUM-ACTIVATED ENZYME SYSTEMS -- 1. Introduction -- 1.1. Chemistry of Magnesium -- 1.2. Magnesium-Ligand Chemistry -- 1.3. Metabolism of Magnesium within Prokaryotic and Eukaryotic Cells -- 2. Known Structures in Magnesium-Activated Enzyme Systems -- 2.1. Bi-Mg2+-Bound Structures -- 2.2. Kinases -- 2.3. Mg2+-Induced Conformational Changes in Proteins -- 3. Unknown Structures -- 3.1. Magnesium-Protoporphyrin IX Chelatase -- 3.2. Sphingomyelinase -- 3.3. Mycobacterial GDP-Mannose Pyrophosphorylase -- 3.4. N1-(5'-Phosphoribosybadenosine-5'-monophosphate Cyclohydrolase -- 4. Structure-Function Relationships -- 4.1. Kinases -- 4.2. DNA Polymerases -- 4.3. p21ms -- 4.4. Ribozymes -- 4.5. Isocitrate Dehydrogenase -- 4.6. Xylose Isomerase -- 5. Conclusions -- Acknowledgments -- Abbreviations -- References -- Chapter 5 CALCIUM AND ITS ENZYMES -- 1. Introduction -- 1.1. Aims and Scope -- 1.2. Coordination Chemistry of Ca2+ -- 1.3. Bioinorganic Role of Ca2+ -- 1.4. Homeostasis and Metabolism -- 1.5. Distribution of Ca2+-Binding Proteins -- 1.6. Introduction to Systems Chosen for Discussion -- 2. Enzymes/Proteins with Known Structure -- 2.1. EF-Hand Proteins -- 2.2. Annexins -- 2.3. C2 Domains -- 2.4. EGF-Like Modules -- 2.5. Lectins -- 3. Enzymes/Proteins with Unknown Structure -- 4. Structure-Function Relationships -- 5. Perspectives -- 6. Ca[sup(2+)] and Protein-Related Internet Resources -- Abbreviations and Definitions -- References -- Chapter 6 VANADIUM IN PROTEINS AND ENZYMES -- 1. Introduction -- 1.1. Coordination Chemistry of Vanadium. , 1.2. Bioinorganic Role of Vanadium -- 2. Vanadium Enzymes with Known Structure: Vanadium Haloperoxidases -- 2.1. Vanadium Chloroperoxidase -- 2.2. Vanadium Bromoperoxidase -- 3. Vanadium Enzymes of Unknown Structure: Vanadium Nitrogenase -- 3.1. Occurrence and Biological Significance -- 3.2. Structural Considerations and Reactivity -- 4. Structure-Function Relationships -- 4.1. Vanadium Haloperoxidase Expression Systems -- 4.2. Comparative Aspects of the Vanadium Sites in V-BrPO and V-C1PO -- 4.3. Mechanistic Considerations of the Catalytic Cycle -- 5. Perspectives -- Acknowledgments -- Abbreviations and Definitions -- References -- Chapter 7 ARE THERE PROTEINS CONTAINING CHROMIUM? -- 1. Introduction -- 2. Enzymes/Proteins with Known Structure -- 3. Enzymes/Proteins with Unknown Structure -- 4. Perspectives -- Abbreviations -- References -- Chapter 8 MANGANESE-CONTAINING ENZYMES AND PROTEINS -- 1. Introduction -- 1.1. Coordination Chemistry of Manganese -- 1.2. Manganese as an Oxidizing/Reducing Agent -- 1.3. Bioinorganic Role of Manganese -- 1.4. Homeostasis and Metabolism -- 2. Enzymes/Proteins with Known Structure -- 2.1. Oxidoreductases -- 2.2. Transferases -- 2.3. Hydrolases -- 2.4. Lyases -- 2.5. Isomerases -- 2.6. Ligases -- 2.7. Proteins Containing Bound Manganese -- 3. Manganese Enzymes with Unknown Structure -- 3.1. Oxidoreductases -- 3.2. Transferases -- 3.3. Hydrolases -- 3.4. Lyases -- 3.5. Isomerases -- 3.6. Ligases -- 3.7. Proteins Containing Bound Manganese -- 4. Structure-Function Relationships -- 4.1. Description of the Coordination Sphere of Manganese in Proteins -- 4.2. Description of Reaction Mechanisms -- 5. Perspectives and Outlook -- Acknowledgments -- Abbreviations -- References -- Chapter 9 IRON IN HEME AND RELATED PROTEINS -- 1. Introduction -- 1.1. Coordination Chemistry of Heme -- 1.2. Biosynthesis of Heme. , 1.3. Bioinorganic Role of Heme -- 2. Enzymes and Proteins with Known Structure -- 2.1. Cytochromes -- 2.2. Globins -- 2.3. Nitrophorin -- 2.4. Heme-Based Biosensors -- 2.5. Catalases -- 2.6. Peroxidases -- 2.7. Cytochrome P450 -- 2.8. Nitric Oxide Synthase -- 2.9. Hydroxylamine Oxidoreductase -- 2.10. Nitrite Reductase -- 2.11. Bacterioferritins -- 2.12. Heme Oxygenase -- 3. Enzymes/Proteins with Unknown Structure -- 3.1. Guanylyl Cyclase -- 3.2. Cystathionine B-Synthase -- 3.3. Indoleamine 2,3-Dioxygenase and Tryptophan 2,3-Dioxygenase -- 4. Structure-Function Relationships -- 4.1. Expression Systems -- 4.2. Detailed Structure-Function Relationships -- 5. Perspectives and Outlook -- 5.1. Why Heme? Evolutionary Aspects -- 5.2. An Outlook -- Acknowledgments -- Abbreviations -- References -- Chapter 10 IRON-SULFUR PROTEINS -- 1. Introduction -- 1.1. Coordination Chemistry of Iron in Iron-Sulfur Proteins -- 1.2. Overview of Consensus Sequences and Structural Classification -- 1.3. Bioinorganic Roles of Clusters -- 2. Iron-Sulfur Proteins with Known Structures -- 2.1. Rubredoxins and Other Proteins with Mononuclear Iron-Sulfur Clusters -- 2.2. Rieske Proteins -- 2.3. 2Fe-2S Ferredoxins -- 2.4. Ferredoxins with FesS4 and/or Fe4S4 Clusters -- 2.5. High Potential Iron-Sulfur Proteins -- 2.6. Aconitase and Iron Regulatory Proteins -- 2.7. Siroheme-Containing Proteins -- 2.8. Nitrogenase Iron Protein -- 2.9. Fe4S4 Cluster-Containing DNA Repair Enzymes -- 2.10. Glutamine Phosphoribosylpyrophosphate Amidotransferase -- 2.11. Trimethylamine Dehydrogenase -- 2.12. The "Hybrid" or "Meatball" Cluster -- 2.13. Fumarate Reductase and Succinate Dehydrogenase -- 2.14. Pyruvate-.Ferredoxin Oxidoreductase -- 3. Relevant Iron-Sulfur Proteins with Unknown Structures -- 3.1. Ribonucleotide Reductase and Pyruvate Formate-Lyase Activase. , 3.2. Biotin Synthase and Related Systems -- 3.3. Ferredoxin:Thioredoxin Reductase -- 3.4. The Regulator of Fumarate and Nitrate Reduction (FNR) -- 3.5. The SoxR Protein -- 4. Structure-Function Relationships -- 4.1. The Role of the Cluster and of the Protein Moieties in Electron Transfer by Iron-Sulfur Proteins -- 4.2. Fe3S4/Fe4S4 Interconversion -- 4.3. Fe4S4/Fe2S4 Conversions -- 4.4. Fe-Only Hydrogenases: The H Cluster -- 4.5. The Role of the Cluster in Folding and Stability of Iron-Sulfur Proteins -- 5. Perspectives -- 5.1. Evolutionary Aspects -- 5.2. Open Questions -- Acknowledgments -- Abbreviations and Definitions -- References -- Chapter 11 STRUCTURE-FUNCTION OF NONHEME IRON PROTEINS WITH OXYGEN- AND NITROGEN-DOMINATED COORDINATION -- 1. Introduction -- 1.1. Iron Homeostasis and Metabolism -- 1.2. Iron and Nonheme Iron Proteins -- 2. Iron-Oxygen/Nitrogen Protein Families -- 2.1. Structural and Mechanistic Studies of Iron-Oxygen/Nitrogen Proteins -- 3. Structure and Mechanisms of Iron-Oxygen/Nitrogen Proteins -- 3.1. Lipoxygenases -- 3.2. Intradiol Dioxygenases -- 3.3. Pterin-Dependent Hydroxylases -- 3.4. 2-Oxoglutarate-Dependent Oxidases and Related Enzymes -- 3.5. Extradiol Dioxygenases and Related Enzymes -- 3.6. Dioxygenases Containing Rieske Centers -- 3.7. Hemerythrin -- 3.8. Large Diiron Carboxylate Proteins -- 3.9. Rubrerythrin -- 3.10. Nitrile Hydratases -- 3.11. Purple Acid Phosphatases -- 4. An Emerging View of the Structure-Function Relationship of Iron-Oxygen/Nitrogen Proteins -- 4.1. Effects of the Coordination Environment -- 4.2. Effects of Net Charge and Charge Distributions -- 4.3. Conformational Flexibility and the Control of O2 Reactivity -- 4.4. Geometries of the Activated O2 Species -- Acknowledgments -- Abbreviations and Definitions -- References -- Chapter 12 IRON STORAGE AND TRANSPORT PROTEINS -- 1. Introduction. , 2. Proteins with Known Structure.