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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, "Overviews of Biological Inorganic Chemistry," 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, "Metal-Ion Containing Biological Systems," 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.

Tabla de contenidos provista por Syndetics

• List of Contributors(p. xix)
• Preface(p. xxiii)
• Acknowledgments(p. xxv)
• Chapter I Introduction and Text Overview(p. 1)
• I.1 The Elements of Life(p. 1)
• I.2 Functional Roles of Biological Inorganic Elements(p. 1)
• I.3 A Guide to This Text(p. 3)
• Part A Overviews of Biological Inorganic Chemistry(p. 5)
• Chapter II Bioinorganic Chemistry and the Biogeochemical Cycles(p. 7)
• II.1 Introduction(p. 7)
• II.2 The Origin and Abundance of the Chemical Elements(p. 8)
• II.3 The Carbon/Oxygen/Hydrogen Cycles(p. 12)
• II.4 The Nitrogen Cycle(p. 16)
• II.5 The Sulfur Cycle(p. 20)
• II.6 The Interaction and Integration of the Cycles(p. 24)
• II.7 Conclusions(p. 29)
• Chapter III Metal Ions and Proteins: Binding, Stability, and Folding(p. 31)
• III.1 Introduction(p. 31)
• III.2 The Metal Cofactor(p. 31)
• III.3 Protein Residues as Ligands for Metal Ions(p. 33)
• III.4 Genome Browsing(p. 37)
• III.5 Folding and Stability of Metalloproteins(p. 37)
• III.6 Kinetic Control of Metal Ion Delivery(p. 40)
• Chapter IV Special Cofactors and Metal Clusters(p. 43)
• IV.1 Why Special Metal Cofactors?(p. 43)
• IV.2 Types of Cofactors, Structural Features, and Occurrence(p. 46)
• IV.3 Cofactor Biosynthesis(p. 54)
• Chapter V Transport and Storage of Metal Ions in Biology(p. 57)
• V.1 Introduction(p. 57)
• V.2 Metal Ion Bioavailability(p. 59)
• V.3 General Properties of Transport Systems(p. 61)
• V.4 Iron Illustrates the Problems of Metal Ion Transport(p. 66)
• V.5 Transport of Metal Ions Other Than Iron(p. 70)
• V.6 Mechanisms of Metal Ion Storage and Resistance(p. 71)
• V.7 Intracellular Metal Ion Transport and Trafficking(p. 74)
• V.8 Summary(p. 76)
• Chapter VI Biominerals and Biomineralization(p. 79)
• VI.1 Introduction(p. 79)
• VI.2 Biominerals: Types and Functions(p. 79)
• VI.3 General Principles of Biomineralization(p. 83)
• VI.4 Conclusions(p. 93)
• Chapter VII Metals in Medicine(p. 95)
• VII.1 Introduction(p. 95)
• VII.2 Metallotherapeutics(p. 96)
• VII.3 Imaging and Diagnosis(p. 114)
• VII.4 Molecular Targets(p. 122)
• VII.5 Metal Metabolism as a Therapeutic Target(p. 129)
• VII.6 Conclusions(p. 132)
• Part B Metal Ion Containing Biological Systems(p. 137)
• Chapter VIII Metal Ion Transport and Storage(p. 139)
• VIII.1 Transferrin(p. 139)
• VIII.1.1 Introduction: Iron Metabolism and the Aqueous Chemistry of Iron(p. 139)
• VIII.1.2 Transferrin: The Iron Transporting Protein of Complex Organisms(p. 140)
• VIII.1.3 Iron-Donating Function of Transferrin(p. 141)
• VIII.1.4 Interaction of Transferrin with HFE(p. 143)
• VIII.2 Ferritin(p. 144)
• VIII.2.1 Introduction: The Need for Ferritins(p. 144)
• VIII.2.2 Ferritin: Nature's Nanoreactor for Iron and Oxygen(p. 145)
• VIII.3 Siderophores(p. 151)
• VIII.3.1 Introduction: The Need for Siderophores(p. 151)
• VIII.3.2 Siderophore Structures(p. 151)
• VIII.3.3 Thermodynamics of Ferric Ion Coordination by Siderophores(p. 152)
• VIII.3.4 Outer-Membrane Receptor Proteins for Ferric Siderophores(p. 153)
• VIII.3.5 Marine Siderophores(p. 154)
• VIII.4 Metallothioneins(p. 156)
• VIII.4.1 Introduction(p. 157)
• VIII.4.2 Classes of Metallothioneins(p. 157)
• VIII.4.3 Induction and Isolation(p. 157)
• VIII.4.4 Structural and Spectroscopic Properties(p. 158)
• VIII.4.5 Reactivity and Function(p. 161)
• VIII.5 Copper-Transporting ATPases(p. 163)
• VIII.5.1 Introduction: Wilson and Menkes Diseases(p. 163)
• VIII.5.2 Structure and Function(p. 163)
• VIII.5.3 Metal Ion Binding and Conformational Changes(p. 165)
• VIII.6 Metallochaperones(p. 166)
• VIII.6.1 Introduction(p. 166)
• VIII.6.2 The Need for Metallochaperones(p. 167)
• VIII.6.3 COX17(p. 169)
• VIII.6.4 ATX1(p. 169)
• VIII.6.5 Copper Chaperone for SOD1(p. 171)
• VIII.6.6 Metallochaperones for Other Metals?(p. 172)
• VIII.6.7 Concluding Remarks(p. 173)
• Chapter IX Hydrolytic Chemistry(p. 175)
• IX.1 Metal-Dependent Lyase and Hydrolase Enzymes. (I) General Metabolism(p. 175)
• IX.1.1 Introduction(p. 175)
• IX.1.2 Magnesium(p. 176)
• IX.1.3 Zinc(p. 179)
• IX.1.4 Manganese(p. 183)
• IX.2 Metal-Dependent Lyase and Hydrolase Enzymes. (II) Nucleic Acid Biochemistry(p. 185)
• IX.2.1 Introduction(p. 185)
• IX.2.2 Magnesium-Dependent Enzymes(p. 185)
• IX.2.3 Calcium(p. 192)
• IX.2.4 Zinc(p. 194)
• IX.3 Urease(p. 198)
• IX.3.1 Introduction(p. 198)
• IX.3.2 The Structure of Native Urease(p. 199)
• IX.3.3 The Structure of Urease Complexed with Transition State and Substrate Analogues(p. 200)
• IX.3.4 The Structure-Based Mechanism(p. 202)
• IX.3.5 The Structure of Urease Complexed with Competitive Inhibitors(p. 204)
• IX.3.6 The Molecular Basis for in vivo Urease Activation and Nickel Trafficking(p. 206)
• IX.4 Aconitase(p. 209)
• IX.4.1 Introduction(p. 209)
• IX.4.2 Stereochemistry of the Citrate-Isocitrate Isomerase Reaction(p. 210)
• IX.4.3 Characterization and Function of the Fe-S Cluster(p. 211)
• IX.4.4 Active Site Amino Acid Residues and the Reaction Mechanism(p. 212)
• IX.4.5 Cluster Reactivity and Cellular Function(p. 214)
• IX.5 Catalytic Nucleic Acids(p. 215)
• IX.5.1 Introduction and Discovery of Catalytic Nucleic Acids(p. 215)
• IX.5.2 Scope and Efficiency of Catalytic Nucleic Acids(p. 216)
• IX.5.3 Classification of Catalytic Nucleic Acids with Hydrolytic Activity(p. 217)
• IX.5.4 Metal Ions as Important Cofactors in Catalytic Nucleic Acids(p. 219)
• IX.5.5 Interactions between Metal Ions and Catalytic Nucleic Acids(p. 221)
• IX.5.6 The Role of Metal Ions in Catalytic Nucleic Acids(p. 222)
• IX.5.7 Expanding the Repertoire of Catalytic Nucleic Acids with Transition Metal Ions(p. 225)
• IX.5.8 Application of Catalytic Nucleic Acids(p. 225)
• IX.5.9 From Metalloproteins to Metallocatalytic Nucleic Acids(p. 226)
• Chapter X Electron Transfer, Respiration, and Photosynthesis(p. 229)
• X.1 Electron-Transfer Proteins(p. 229)
• X.1.1 Introduction(p. 229)
• X.1.2 Determinants of Reduction Potentials(p. 230)
• X.1.3 Iron-Sulfur Proteins(p. 239)
• X.1.4 Cytochromes(p. 245)
• X.1.5 Copper Proteins(p. 250)
• X.1.6 A Further Comment on the Size of the Cofactor(p. 254)
• X.1.7 Donor-Acceptor Interactions(p. 255)
• X.2 Electron Transfer through Proteins(p. 261)
• X.2.1 Introduction(p. 261)
• X.2.2 Basic Concepts(p. 261)
• X.2.3 Semiclassical Theory of Electron Transfer(p. 264)
• X.3 Photosynthesis and Respiration(p. 278)
• X.3.1 Introduction(p. 278)
• X.3.2 Qualitative Aspects of Mitchell's Chemiosmotic Hypothesis for Phosphorylation(p. 279)
• X.3.3 An Interlude: Reduction Potentials(p. 279)
• X.3.4 Maximizing Free Energy and ATP Production(p. 281)
• X.3.5 Quantitative Aspects of Mitchell's Chemiosmotic Hypothesis for Phosphorylation(p. 283)
• X.3.6 Cellular Structures Involved in the Energy Transduction Process: Similarities among Bacteria, Mitochondria, and Chloroplasts(p. 284)
• X.3.7 The Respiratory Chain(p. 285)
• X.3.8 The Photosynthetic Electron-Transfer Chain(p. 291)
• X.3.9 A Common Underlying Theme in Biological O[subscript 2]/H[subscript 2]O Metabolism: Metalloradical Active Sites(p. 299)
• X.4 Dioxygen Production: Photosystem II(p. 302)
• X.4.1 Introduction(p. 302)
• X.4.2 Photosystem II Activity: Light-Catalyzed Two- and Four-Electron Redox Chemistry(p. 303)
• X.4.3 Photosystem II Protein Structure and Redox Cofactors(p. 305)
• X.4.4 Inorganic Ions of PSII(p. 308)
• X.4.5 Modeling the Structure of the PSII Mn Cluster(p. 313)
• X.4.6 Proposals for the Mechanism of Photosynthetic Water Oxidation(p. 314)
• Chapter XI Oxygen Metabolism(p. 319)
• XI.1 Dioxygen Reactivity and Toxicity(p. 319)
• XI.1.1 Introduction(p. 319)
• XI.1.2 Chemistry of Dioxygen(p. 320)
• XI.1.3 Dioxygen Toxicity(p. 325)
• XI.2 Superoxide Dismutases and Reductases(p. 331)
• XI.2.1 Introduction(p. 331)
• XI.2.2 Superoxide Chemistry(p. 332)
• XI.2.3 Superoxide Dismutase and Superoxide Reductase Mechanistic Principles(p. 333)
• XI.2.4 Superoxide Dismutase and Superoxide Reductase Enzymes(p. 335)
• XI.3 Peroxidase and Catalases(p. 343)
• XI.3.1 Introduction(p. 343)
• XI.3.2 Overall Structure(p. 344)
• XI.3.3 Active-Site Structure(p. 345)
• XI.3.4 Mechanism(p. 346)
• XI.3.5 Reduction of Compounds I and II(p. 350)
• XI.4 Dioxygen Carriers(p. 354)
• XI.4.1 Introduction: Biological Dioxygen Transport Systems(p. 354)
• XI.4.2 Thermodynamic and Kinetic Aspects of Dioxygen Transport(p. 357)
• XI.4.3 Cooperativity and Dioxygen Transport(p. 358)
• XI.4.4 Biological Dioxygen Carriers(p. 361)
• XI.4.5 Protein Control of the Chemistry of Dioxygen, Iron, Copper, and Cobalt(p. 370)
• XI.4.6 Structural Basis of Ligand Affinities of Dioxygen Carriers(p. 377)
• XI.4.7 Final Remarks(p. 385)
• XI.5 Dioxygen Activating Enzymes(p. 388)
• XI.5.1 Introduction: Converting Carriers into Activators(p. 388)
• XI.5.2 Mononuclear Nonheme Metal Centers That Activate Dioxygen(p. 400)
• XI.6 Reducing Dioxygen to Water: Cytochrome c Oxidase(p. 413)
• XI.6.1 Introduction(p. 414)
• XI.6.2 Lessons from the X-Ray Structures of Bovine Heart Cytochrome c Oxidase(p. 415)
• XI.6.3 Reaction Mechanism(p. 419)
• XI.7 Reducing Dioxygen to Water: Multi-Copper Oxidases(p. 427)
• XI.7.1 Introduction(p. 427)
• XI.7.2 Occurrence and General Properties(p. 427)
• XI.7.3 Functions(p. 428)
• XI.7.4 X-Ray Structures(p. 429)
• XI.7.5 Structure-Function Relationships(p. 435)
• XI.7.6 Perspectives(p. 437)
• XI.8 Reducing Dioxygen to Water: Mechanistic Considerations(p. 440)
• Chapter XII Hydrogen, Carbon, and Sulfur Metabolism(p. 443)
• XII.1 Hydrogen Metabolism and Hydrogenase(p. 443)
• XII.1.1 Introduction: Microbiology and Biochemistry of Hydrogen(p. 443)
• XII.1.2 Hydrogenase Structures(p. 444)
• XII.1.3 Biosynthesis(p. 447)
• XII.1.4 Hydrogenase Reaction Mechanism(p. 447)
• XII.1.5 Regulation by Hydrogen(p. 450)
• XII.2 Metalloenzymes in the Reduction of One-Carbon Compounds(p. 452)
• XII.2.1 Introduction: Metalloenzymes in the Reduction of One-Carbon Compounds to Methane and Acetic Acid(p. 452)
• XII.2.2 Electron Donors and Acceptors for One-Carbon Redox Reactions(p. 455)
• XII.2.3 Conversion to the "Formate" Oxidation Level by Two-Electron Reduction of Carbon Dioxide(p. 455)
• XII.2.4 Conversion from the "Formate" through the "Formaldehyde" to the "Methanol" Oxidation Level(p. 458)
• XII.2.5 Interconversions at the Methyl Level: Methyltransferases(p. 459)
• XII.2.6 Methyl Group Reduction or Carbonylation(p. 461)
• XII.2.7 Summary(p. 464)
• XII.3 Biological Nitrogen Fixation and Nitrification(p. 468)
• XII.3.1 Introduction(p. 468)
• XII.3.2 Biological Nitrogen Fixation: When and How Did Biological Nitrogen Fixation Evolve?(p. 469)
• XII.3.3 Nitrogen-Fixing Organisms and Crop Plants(p. 470)
• XII.3.4 Relationships among Nitrogenases(p. 471)
• XII.3.5 Structures of the Mo-Nitrogenase Component Proteins and Their Complex(p. 474)
• XII.3.6 Mechanism of Nitrogenase Action(p. 480)
• XII.3.7 Future Perspectives for Nitrogen Fixation(p. 485)
• XII.3.8 Biological Nitrification: What Is Nitrification?(p. 485)
• XII.3.9 Enzymes Involved in Nitrification by Autotrophic Organisms(p. 485)
• XII.3.10 Nitrification by Heterotrophic Organisms(p. 490)
• XII.3.11 Anaerobic Ammonia Oxidation (Anammox)(p. 491)
• XII.3.12 Future Perspectives for Nitrification(p. 491)
• XII.4 Nitrogen Metabolism: Denitrification(p. 494)
• XII.4.1 Introduction(p. 494)
• XII.4.2 The Enzymes of Denitrification(p. 494)
• XII.4.3 Summary(p. 505)
• XII.5 Sulfur Metabolism(p. 508)
• XII.5.1 Introduction(p. 508)
• XII.5.2 Biological Role of Sulfur Compounds(p. 509)
• XII.5.3 Biological Sulfur Cycle(p. 510)
• XII.6 Molybdenum Enzymes(p. 518)
• XII.6.1 Introduction(p. 518)
• XII.6.2 The Active Sites of the Molybdenum Enzymes(p. 521)
• XII.6.3 Molybdenum Enzymes(p. 530)
• XII.6.4 Conclusions(p. 542)
• XII.7 Tungsten Enzymes(p. 545)
• XII.7.1 Introduction(p. 545)
• XII.7.2 Biochemical Properties of Tungstoenzymes(p. 546)
• XII.7.3 Structural Properties of Tungstoenzymes(p. 550)
• XII.7.4 Spectroscopic Properties of Tungstoenzymes(p. 552)
• XII.7.5 Mechanism of Action of Tungstoenzymes(p. 553)
• XII.7.6 Tungsten Model Complexes(p. 554)
• XII.7.7 Tungsten versus Molybdenum(p. 555)
• Chapter XIII Metalloenzymes with Radical Intermediates(p. 557)
• XIII.1 Introduction to Free Radicals(p. 557)
• XIII.1.1 Introduction(p. 557)
• XIII.1.2 Free Radical Stability and Reactivity(p. 559)
• XIII.1.3 Electron Paramagnetic Resonance Spectroscopy(p. 560)
• XIII.1.4 Biological Radical Complexes(p. 560)
• XIII.2 Cobalamins(p. 562)
• XIII.2.1 Introduction(p. 562)
• XIII.2.2 Nomenclature and Chemistry(p. 562)
• XIII.2.3 Enzyme Systems Using AdoCbl(p. 565)
• XIII.2.4 Unresolved Issues in AdoCbl Requiring Enzymes(p. 569)
• XIII.2.5 MeCbl Using Methionine Synthase as a Case Study(p. 570)
• XIII.2.6 Unresolved Issues in Methyl Transfer Reactions with MeCbl(p. 572)
• XIII.3 Ribonucleotide Reductases(p. 575)
• XIII.3.1 Introduction: Three Classes of Ribonucleotide Reductases(p. 575)
• XIII.3.2 Mechanisms of Radical Formation(p. 577)
• XIII.3.3 Conclusions(p. 580)
• XIII.4 Fe-S Clusters in Radical Generation(p. 582)
• XIII.4.1 Introduction(p. 582)
• XIII.4.2 Glycyl Radical Generation(p. 586)
• XIII.4.3 Isomerization Reactions(p. 589)
• XIII.4.4 Cofactor Biosynthesis(p. 590)
• XIII.4.5 DNA Repair(p. 592)
• XIII.4.6 Radical-SAM Enzymes: Unifying Themes(p. 593)
• XIII.5 Galactose Oxidase(p. 595)
• XIII.5.1 Introduction(p. 595)
• XIII.5.2 Active Site Structure(p. 596)
• XIII.5.3 Oxidation-Reduction Chemistry(p. 597)
• XIII.5.4 Catalytic Turnover Mechanism(p. 598)
• XIII.5.5 Mechanism of Cofactor Biogenesis(p. 600)
• XIII.6 Amine Oxidases(p. 601)
• XIII.6.1 Introduction(p. 601)
• XIII.6.2 Structural Characterization(p. 602)
• XIII.6.3 Structure-Function Relationship(p. 604)
• XIII.6.4 Mechanistic Considerations(p. 604)
• XIII.6.5 Biogenesis of Amine Oxidases(p. 606)
• XIII.6.6 Conclusion(p. 606)
• XIII.7 Lipoxygenase(p. 607)
• XIII.7.1 Introduction(p. 607)
• XIII.7.2 Structure(p. 608)
• XIII.7.3 Mechanism(p. 608)
• XIII.7.4 Kinetics(p. 611)
• Chapter XIV Metal Ion Receptors and Signaling(p. 613)
• XIV.1 Metalloregulatory Proteins(p. 613)
• XIV.1.1 Introduction: Structural Metal Sites(p. 613)
• XIV.1.2 Structural Zn Domains(p. 614)
• XIV.1.3 Metal Ion Signaling(p. 618)
• XIV.1.4 Metalloregulatory Proteins(p. 620)
• XIV.1.5 Metalloregulation of Transcription(p. 620)
• XIV.1.6 Metalloregulation of Post-Transcriptional Processes(p. 625)
• XIV.1.7 Post-Translational Metalloregulation(p. 626)
• XIV.2 Structural Zinc-Binding Domains(p. 628)
• XIV.2.1 Introduction(p. 628)
• XIV.2.2 Molecular and Macromolecular Interactions(p. 628)
• XIV.2.3 Metal Coordination and Substitution(p. 630)
• XIV.2.4 Zinc Fingers and Protein Design(p. 632)
• XIV.3 Calcium in Mammalian Cells(p. 635)
• XIV.3.1 Introduction(p. 635)
• XIV.3.2 Concentration Levels of Ca[superscript 2+] in Higher Organisms(p. 635)
• XIV.3.3 The Intracellular Ca[superscript 2+]-Signaling System(p. 636)
• XIV.3.4 A Widespread Ca[superscript 2+]-Binding Motif: The EF-Hand(p. 639)
• XIV.3.5 Ca[superscript 2+] Induced Structural Changes in Modulator Proteins (Calmodulin, Troponin C)(p. 641)
• XIV.3.6 Ca[superscript 2+] Binding in Buffer or Transporter Proteins(p. 645)
• XIV.4 Nitric Oxide(p. 647)
• XIV.4.1 Introduction: Physiological Role and Chemistry of Nitric Oxide(p. 647)
• XIV.4.2 Chemistry of Oxygen Activation(p. 649)
• XIV.4.3 Overview of Nitric Oxide Synthase Architecture(p. 650)
• XIV.4.4 Nitric Oxide Synthase Mechanism(p. 651)
• Cell Biology, Biochemistry, and Evolution: Tutorial I(p. 657)
• T.I.1 Life's Diversity(p. 657)
• T.I.2 Evolutionary History(p. 666)
• T.I.3 Genomes and Proteomes(p. 668)
• T.I.4 Cellular Components(p. 670)
• T.I.5 Metabolism(p. 685)
• Fundamentals of Coordination Chemistry: Tutorial II(p. 695)
• T.II.1 Introduction(p. 695)
• T.II.2 Complexation Equilibria in Water(p. 695)
• T.II.3 The Effect of Metal Ions on the pK[subscript a] of Ligands(p. 698)
• T.II.4 Ligand Specificity: Hard versus Soft(p. 698)
• T.II.5 Coordination Chemistry and Ligand-Field Theory(p. 700)
• T.II.6 Consequences of Ligand-Field Theory(p. 703)
• T.II.7 Kinetic Aspects of Metal Ion Binding(p. 708)
• T.II.8 Redox Potentials and Electron-Transfer Reactions(p. 709)
• Appendix I Abbreviations(p. 713)
• Appendix II Glossary(p. 717)
• Appendix III The Literature of Biological Inorganic Chemistry(p. 727)
• Appendix IV Introduction to the Protein Data Bank (PDB)(p. 729)
• Index(p. 731)

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CHOICE Review

This is an important compendium of most material in the interdisciplinary field of bioinorganic chemistry. Because readers might not be well versed in both the biological and the inorganic aspect of the chapters, the authors have included two well-written and complete chapters ("tutorials") that summarize essential features of biological and inorganic coordination chemistry. In addition, there are valuable appendixes that include a glossary and abbreviations used in biological chemistry, as well as an introduction to the Protein Data Bank (PDB). Part A of the book includes chapters of a more introductory nature and is generally clearly written. Part B offers a more detailed look at specific bioinorganic topics; this part is certain to have material added to it for future editions. Chapters are written by specialists in the field, with many references at the end of each chapter; they invite further research by readers and are useful for students. Much of the book treats macromolecules that incorporate a metal in a structural or reactive role (whose structures are best seen using the PDB), but there are chapters dealing with medicinal bioinorganic compounds and biomineralization. An indispensable book for novices. Summing Up: Highly recommended. Upper-division undergraduates through professionals. M. Rossi Vassar College