Concepts and models in bioinorganic chemistry

Abstract

Foreword. Preface. List of Contributors. Abbreviations. 1 The Biodistribution of Metal Ions (Robert J. P. Williams). 1.1 Introduction. 1.2 Rates of Exchange. 1.3 The Limitations of Water as a Solvent. 1.4 Equilibrium: Values of Binding Constants. 1.5 Quantitative Metal Ion Equilibria: Donor Strength. 1.6 The Effect of Size and Charge of Metal Ions. 1.7 The Effect of Electron Affi nity. 1.8 Control over Ligand Concentration. 1.9 The Compartments of Organisms. 1.10 Transport. 1.11 The Irreversible Binding of Fe, Co, Ni, Mg, and Mo (W). 1.12 Vanadium, Molybdenum, and Tungsten. 1.13 Rates of Exchange. 1.14 Summary. 2 Medicinal Inorganic Chemistry (Katherine H. Thompson and Chris Orvig). 2.1 Introduction. 2.2 Key Developments. 2.3 Summary of Key Concepts. 2.4 Selected Current Research Directions. 2.5 Open Questions. 3 The Chemical Toxicology of Metals and Metalloids (Graham N. George). 3.1 Introduction. 3.2 Arsenic. 3.3 Mercury. 3.4 Chromium. 3.5 The Promise of New Techniques. 4 Theoretical Modeling of Redox Processes in Enzymes and Biomimetic Systems (Arianna Bassan, Tomasz Borowski, Marcus Lundberg, and Per E. M. Siegbahn). 4.1 Introduction. 4.2 Computational Model. 4.3 Nonheme Iron Active Sites That Perform Alkane Hydroxylation and Olefin Oxidation. 4.4 Keto Acid-Dependent Dioxygenases and Their Synthetic Analogues. 4.5 Copper Complexes in Enzymes and Synthetic Systems. 4.6 Manganese Complexes That Oxidize Water to Dioxygen. 4.7 Conclusions. 5 Charge Transport in Biological Molecules (Yitao Long and Heinz-Bernhard Kraatz). 5.1 Introduction. 5.2 Electron Transfer in Proteins. 5.3 Electron Transfer in Peptides. 5.4 Charge Transfer in DNA. 5.5 Summary and Open Questions. 6 Bioorganometallic Chemistry (Nils Metzler-Nolte and Kay Severin). 6.1 Introduction. 6.2 Organometallic Complexes in Nature. 6.3 Synthetic Organometallic Complexes with Bioligands. 6.4 Organometallic Pharmaceuticals. 6.5 Analytical Bioorganometallic Chemistry. 6.6 Bioorganometallic Catalysis. 6.7 Conclusions and Outlook. 7 The Bioinorganic Side of Nucleic Acid Chemistry: Interactions with Metal Ions (Bernhard Lippert and Jens Muller). 7.1 Introduction: Nucleic Acids and Metals. 7.2 Modeling Metal-Nucleic Acid Interactions. 7.3 Take-Home Message. 7.4 Open Questions and Perspectives. 8 Nuclease and Peptidase Models (Srecko I. Kirin, Roland Kramer, and Nils Metzler-Nolte). 8.1 Introduction. 8.2 Mechanistic Considerations. 8.3 Substrates for Model Studies. 8.4 Peptidase Models. 8.5 Nuclease Models. 8.6 Applications. 9 Metalloporphyrins, Metalloporphyrinoids, and Model Systems (Bernhard Krautler and Bernhard Jaun). 9.1 Introduction: Biological Background. 9.2 Model Systems and Model Compounds to Understand Biological Function. 9.3 Summary of Key Concepts. 9.4 Open Questions and the Direction of Future Research. 10 Model Complexes for Vanadium-Containing Enzymes (Dieter Rehder). 10.1 Biological Background and Motivation. 10.2 Model Compounds. 10.3 Summary of Key Concepts. 10.4 Open Questions and the Direction of Future Research. 11 Model Complexes for Molybdenum- and Tungsten-Containing Enzymes (John H. Enemark and J. Jon A. Cooney). 11.1 Biological Background and Motivation. 11.1.1 Introduction 238 11.2 Model Compounds. 11.3 Summary. 11.4 Open Questions. 12 Structural and Functional Models for Oxygen-Activating Nonheme Iron Enzymes (Timothy A. Jackson and Lawrence Que, Jr.). 12.1 Biological Background and Motivation. 12.2 Dinuclear Iron Centers. 12.3 Diiron Models. 12.4 Monoiron Active Sites with a 2-His-1-Carboxylate Facial Triad Motif. 12.5 Monoiron Models. 12.6 Summary of Key Concepts. 12.7 Open Questions and the Direction of Future Research. 13 Model Chemistry of the Iron-Sulfur Protein Active Sites (George A. Koutsantonis). 13.1 Introduction. 13.2 Basic Iron and Sulfur Chemistry. 13.3 Common Iron-Sulfur Geometries. 13.4 Required Protein and Peptide Coordination Environments. 13.5 Syntheses of Model Compounds. 13.6 Properties of Analogues and Their Relation to Protein-Bound Clusters. 13.7 Conclusions. 14 Model Complexes of Ni-Containing Enzymes (Todd C. Harrop and Pradip K. Mascharak). 14.1 Introduction. 14.2 Urease. 14.3 NiFe Hydrogenase. 14.4 Carbon Monoxide Dehydrogenase/Acetyl Coenzyme A Synthase (CODH/ACS). 14.5 Conclusions. 15 Hydrogenases and Model Complexes (Robert H. Morris). 15.1 Introduction. 15.2 What are Hydrogenases? 15.3 Nickel-Iron (NiFe-Hase) and Nickel-Iron-Selenium (NiFeSe-Hase) Hydrogenases. 15.4 Iron-Iron Hydrogenases. 15.5 Similarities and Differences between NiFe-Hase and FeFe-Hase. 15.6 Synthetic Complexes that Model Hydrogenases. 15.7 Conclusions. 15.8 Open Questions and the Direction of Future Research. 16 Model Complexes for Copper-Containing Enzymes (Yunho Lee and Kenneth D. Karlin). 16.1 Introduction. 16.2 Biological Background: Copper Proteins and Motivation for Biomimetic Studies. 16.3 Model Compounds. 16.4 Summary of Key Concepts. 16.5 Open Questions and Directions for Future Research. 17 Model Complexes for Zinc-