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An updated, practical guide to bioinorganic chemistry

Bioinorganic Chemistry: A Short Course, Second Edition provides the fundamentals of inorganic chemistry and biochemistry relevant to understanding bioinorganic topics. Rather than striving to provide a broad overview of the whole, rapidly expanding field, this resource provides essential background material, followed by detailed information on selected topics. The goal is to give readers the background, tools, and skills to research and study bioinorganic topics of special interest to them. This extensively updated premier reference and text: Presents review chapters on the essentials of inorganic chemistry and biochemistry Includes up-to-date information on instrumental and analytical techniques and computer-aided modeling and visualization programs Familiarizes readers with the primary literature sources and online resources Includes detailed coverage of Group 1 and 2 metal ions, concentrating on biological molecules that feature sodium, potassium, magnesium, and calcium ions Describes proteins and enzymes with iron-containing porphyrin ligand systems-myoglobin, hemoglobin, and the ubiquitous cytochrome metalloenzymes-and the non-heme, iron-containing proteins aconitase and methane monooxygenase Appropriate for one-semester bioinorganic chemistry courses for chemistry, biochemistry, and biology majors, this text is ideal for upper-level undergraduate and beginning graduate students. It is also a valuable reference for practitioners and researchers who need a general introduction to bioinorganic chemistry, as well as chemists who want an accessible desk reference.

Tabla de contenidos provista por Syndetics

• Preface(p. xiii)
• Acknowledgments(p. xix)
• 1 Inorganic Chemistry Essentials(p. 1)
• 1.1 Introduction(p. 1)
• 1.2 Essential Chemical Elements(p. 1)
• 1.3 Metals in Biological Systems: A Survey(p. 3)
• 1.4 Inorganic Chemistry Basics(p. 6)
• 1.5 Biological Metal Ion Complexation(p. 8)
• 1.5.1 Thermodynamics(p. 8)
• 1.5.2 Kinetics(p. 9)
• 1.6 Electronic and Geometric Structures of Metals in Biological Systems(p. 13)
• 1.7 Bioorganometallic Chemistry(p. 19)
• 1.8 Electron Transfer(p. 22)
• 1.9 Conclusions(p. 26)
• References(p. 27)
• 2 Biochemistry Fundamentals(p. 29)
• 2.1 Introduction(p. 29)
• 2.2 Proteins(p. 30)
• 2.2.1 Amino Acid Building Blocks(p. 30)
• 2.2.2 Protein Structure(p. 33)
• 2.2.3 Protein Sequencing and Proteomics(p. 39)
• 2.2.4 Protein Function, Enzymes, and Enzyme Kinetics(p. 43)
• 2.3 Nucleic Acids(p. 47)
• 2.3.1 DNA and RNA Building Blocks(p. 47)
• 2.3.2 DNA and RNA Molecular Structures(p. 47)
• 2.3.3 Transmission of Genetic Information(p. 53)
• 2.3.4 Genetic Mutations and Site-Directed Mutagenesis(p. 56)
• 2.3.5 Genes and Cloning(p. 58)
• 2.3.6 Genomics and the Human Genome(p. 61)
• 2.4 Zinc-Finger Proteins(p. 63)
• 2.4.1 Descriptive Examples(p. 67)
• 2.5 Summary and Conclusions(p. 73)
• References(p. 74)
• 3 Instrumental Methods(p. 76)
• 3.1 Introduction(p. 76)
• 3.1.1 Analytical Instrument-Based Methods(p. 76)
• 3.1.2 Spectroscopy(p. 77)
• 3.2 X-Ray Absorption Spectroscopy (XAS) and Extended X-Ray Absorption Fine Structure (EXAFS)(p. 78)
• 3.2.1 Theoretical Aspects and Hardware(p. 78)
• 3.2.2 Descriptive Examples(p. 81)
• 3.3 X-Ray Crystallography(p. 83)
• 3.3.1 Introduction(p. 83)
• 3.3.2 Crystallization and Crystal Habits(p. 84)
• 3.3.3 Theory and Hardware(p. 88)
• 3.3.4 Descriptive Examples(p. 95)
• 3.4 Nuclear Magnetic Resonance(p. 98)
• 3.4.1 Theoretical Aspects(p. 98)
• 3.4.2 Nuclear Screening and the Chemical Shift(p. 101)
• 3.4.3 Spin-Spin Coupling(p. 104)
• 3.4.4 Techniques of Spectral Integration and Spin-Spin Decoupling(p. 106)
• 3.4.5 Nuclear Magnetic Relaxation(p. 107)
• 3.4.6 The Nuclear Overhauser Effect (NOE)(p. 108)
• 3.4.7 Obtaining the NMR Spectrum(p. 110)
• 3.4.8 Two-Dimensional (2D) NMR Spectroscopy(p. 111)
• 3.4.9 Two-Dimensional Correlation Spectroscopy (COSY) and Total Correlation Spectroscopy (TOCSY)(p. 112)
• 3.4.10 Nuclear Overhauser Effect Spectroscopy (NOESY)(p. 115)
• 3.4.11 Multidimensional NMR(p. 116)
• 3.4.12 Descriptive Examples(p. 117)
• 3.5 Electron Paramagnetic Resonance(p. 122)
• 3.5.1 Theory and Determination of g-Values(p. 122)
• 3.5.2 Hyperfine and Superhyperfine Interactions(p. 127)
• 3.5.3 Electron Nuclear Double Resonance (ENDOR) and Electron Spin-Echo Envelope Modulation (ESEEM)(p. 129)
• 3.5.4 Descriptive Examples(p. 129)
• 3.6 Mossbauer Spectroscopy(p. 132)
• 3.6.1 Theoretical Aspects(p. 132)
• 3.6.2 Quadrupole Splitting and the Isomer Shift(p. 134)
• 3.6.3 Magnetic Hyperfine Interactions(p. 136)
• 3.6.4 Descriptive Examples(p. 137)
• 3.7 Other Instrumental Methods(p. 139)
• 3.7.1 Atomic Force Microscopy(p. 139)
• 3.7.2 Fast and Time-Resolved Methods(p. 143)
• 3.7.2.1 Stopped-Flow Kinetic Methods(p. 143)
• 3.7.2.2 Flash Photolysis(p. 144)
• 3.7.2.3 Time-Resolved Crystallography(p. 146)
• 3.7.3 Mass Spectrometry(p. 148)
• 3.8 Summary and Conclusions(p. 153)
• References(p. 154)
• 4 Computer Hardware, Software, and Computational Chemistry Methods(p. 157)
• 4.1 Introduction to Computer-Based Methods(p. 157)
• 4.2 Computer Hardware(p. 157)
• 4.3 Molecular Modeling and Molecular Mechanics(p. 160)
• 4.3.1 Introduction to MM(p. 160)
• 4.3.2 Molecular Modeling, Molecular Mechanics, and Molecular Dynamics(p. 161)
• 4.3.3 Biomolecule Modeling(p. 166)
• 4.3.4 A Molecular Modeling Descriptive Example(p. 167)
• 4.4 Quantum Mechanics-Based Computational Methods(p. 170)
• 4.4.1 Introduction(p. 170)
• 4.4.2 Ab Initio Methods(p. 170)
• 4.4.3 Density Function Theory(p. 171)
• 4.4.4 Semiempirical Methods(p. 173)
• 4.5 Computer Software for Chemistry(p. 174)
• 4.5.1 Mathematical Software(p. 180)
• 4.6 World Wide Web Online Resources(p. 181)
• 4.6.1 Nomenclature and Visualization Resources(p. 181)
• 4.6.2 Online Societies, Online Literature Searching, and Materials and Equipment Websites(p. 183)
• 4.7 Summary and Conclusions(p. 185)
• References(p. 185)
• 5 Group I and II Metals in Biological Systems: Homeostasis and Group I Biomolecules(p. 189)
• 5.1 Introduction(p. 189)
• 5.2 Homeostasis of Metals (and Some Nonmetals)(p. 192)
• 5.2.1 Phosphorus as Phosphate(p. 192)
• 5.2.2 Potassium, Sodium, and Chloride Ions(p. 193)
• 5.2.3 Calcium Homeostasis(p. 194)
• 5.3 Movement of Molecules and Ions Across Membranes(p. 195)
• 5.3.1 Passive Diffusion(p. 195)
• 5.3.2 Facilitated Diffusion(p. 197)
• 5.3.2.1 Gated Channels(p. 197)
• 5.3.3 Active Transport-Ion Pumps(p. 197)
• 5.4 Potassium-Dependent Molecules(p. 199)
• 5.4.1 Na[superscript +]/K[superscript +] ATPase: The Sodium Pump(p. 199)
• 5.4.2 Potassium (K[superscript +]) Ion Channels(p. 203)
• 5.4.2.1 Introduction(p. 203)
• 5.4.2.2 X-Ray Crystallographic Studies(p. 205)
• 5.5 Conclusions(p. 235)
• References(p. 235)
• 6 Group I and II Metals in Biological Systems: Group II(p. 238)
• 6.1 Introduction(p. 238)
• 6.2 Magnesium and Catalytic RNA(p. 238)
• 6.2.1 Introduction(p. 238)
• 6.2.2 Analyzing the Role of the Metal Ion(p. 241)
• 6.2.3 The Group I Intron Ribozyme(p. 244)
• 6.2.4 The Hammerhead Ribozyme(p. 261)
• 6.3 Calcium-Dependent Molecules(p. 301)
• 6.3.1 Introduction(p. 301)
• 6.3.2 Calmodulin(p. 302)
• 6.3.2.1 Introduction(p. 302)
• 6.3.2.2 Calmodulin Structure by X-Ray and NMR(p. 303)
• 6.3.2.3 Calmodulin Interactions with Drug Molecules(p. 308)
• 6.3.2.4 Calmodulin-Peptide Binding(p. 313)
• 6.3.2.5 Conclusions(p. 326)
• 6.4 Phosphoryl Transfer: P-Type ATPases(p. 327)
• 6.4.1 Introduction(p. 327)
• 6.4.2 Calcium P-Type ATPases(p. 327)
• 6.4.2.1 Ca[superscript 2+]-ATPase Protein SERCA1a and the Ca[superscript 2+]-ATPase Cycle(p. 329)
• 6.5 Conclusions(p. 337)
• References(p. 338)
• 7 Iron-Containing Proteins and Enzymes(p. 343)
• 7.1 Introduction: Iron-Containing Proteins with Porphyrin Ligand Systems(p. 343)
• 7.2 Myoglobin and Hemoglobin(p. 343)
• 7.2.1 Myoglobin and Hemoglobin Basics(p. 345)
• 7.2.2 Structure of the Heme Prosthetic Group(p. 347)
• 7.2.3 Behavior of Dioxygen Bound to Metals(p. 348)
• 7.2.4 Structure of the Active Site in Myoglobin and Hemoglobin: Comparison to Model Compounds(p. 349)
• 7.2.5 Some Notes on Model Compounds(p. 352)
• 7.2.6 Iron-Containing Model Compounds(p. 353)
• 7.2.7 Binding of CO to Myoglobin, Hemoglobin, and Model Compounds(p. 356)
• 7.2.8 Conclusions(p. 359)
• 7.3 Introduction to Cytochromes(p. 359)
• 7.4 Cytochrome P450: A Monooxygenase(p. 361)
• 7.4.1 Introduction(p. 361)
• 7.4.2 Cytochrome P450: Structure and Function(p. 363)
• 7.4.3 Cytochrome P450: Mechanism of Activity(p. 365)
• 7.4.4 Analytical Methods: X-Ray Crystallography(p. 369)
• 7.4.5 Cytochrome P450 Model Compounds(p. 372)
• 7.4.5.1 Introduction(p. 372)
• 7.4.5.2 A Cytochrome P450 Model Compound: Structural(p. 372)
• 7.4.5.3 Cytochrome P450 Model Compounds: Functional(p. 374)
• 7.4.6 Cytochrome P450 Conclusions(p. 382)
• 7.5 Cytochrome b(6)f: A Green Plant Cytochrome(p. 382)
• 7.5.1 Introduction(p. 382)
• 7.5.2 Cytochrome b(6)f Metal Cofactor Specifics(p. 386)
• 7.6 Cytochrome bc[subscript 1]: A Bacterial Cytochrome(p. 388)
• 7.6.1 Introduction(p. 388)
• 7.6.2 Cytochrome bc[subscript 1] Structure(p. 389)
• 7.6.3 Cytochrome bc[subscript 1] Metal Cofactor Specifics(p. 391)
• 7.6.4 The Cytochrome bc[subscript 1] Q Cycle(p. 395)
• 7.6.5 Cytochrome bc[subscript 1] Inhibitors(p. 397)
• 7.6.6 Cytochrome bc[subscript 1] Conclusions(p. 408)
• 7.7 Cytochromes c(p. 408)
• 7.7.1 Introduction(p. 408)
• 7.7.2 Mitochondrial Cytochrome c (Yeast)(p. 411)
• 7.7.3 Mitochondrial Cytochrome c (Horse)(p. 416)
• 7.7.4 Cytochrome c Folding, Electron Transfer, and Cell Apoptosis(p. 422)
• 7.7.4.1 Cytochrome c Folding(p. 422)
• 7.7.4.2 Electron Transfer in Cytochrome c and Its Redox Partners(p. 424)
• 7.7.4.3 Apoptosis(p. 427)
• 7.7.5 Cytochrome c Conclusions(p. 429)
• 7.8 Cytochrome c Oxidase(p. 429)
• 7.8.1 Introduction(p. 429)
• 7.8.2 Metal-Binding Sites in Cytochrome c Oxidase(p. 432)
• 7.8.3 Dioxygen Binding, Proton Translocation, and Electron Transport(p. 434)
• 7.8.4 Cytochrome c Oxidase Model Compounds and Associated Analytical Techniques(p. 440)
• 7.8.5 Cytochrome c Oxidase Conclusions(p. 453)
• 7.9 Non-Heme Iron-Containing Proteins(p. 454)
• 7.9.1 Introduction(p. 454)
• 7.9.2 Proteins with Iron-Sulfur Clusters(p. 454)
• 7.9.2.1 The Enzyme Aconitase(p. 455)
• 7.9.3 Iron-Oxo Proteins(p. 458)
• 7.9.3.1 Methane Monooxygenases(p. 459)
• 7.10 Conclusions(p. 465)
• References(p. 466)
• Index(p. 477)

Reseñas proporcionadas por Syndetics

CHOICE Review

This book by Roat-Malone (Washington College, MD) fills a unique niche. Typical undergraduates are not exposed to bioinorganic chemistry because they often lack the requisite biochemical or inorganic chemistry knowledge needed to delve into this area. After reviewing the first edition (CH, May'03, 40-5232), this reviewer adopted the work as a supplemental resource for an advanced undergraduate inorganic chemistry course. The biological importance of inorganic atoms in biological systems had been understudied for quite some time, as evidenced by the fact that leading inorganic works usually devoted only one small chapter to the importance of transition metals in select enzymatic systems. Today there is an impressive amount of bioinorganic research published monthly. The scholar who explores this subject is typically a biochemist self-taught in the subtleties of transition metal coordination chemistry or an inorganic chemist self-taught in biochemistry. The average undergraduate student is neither. This volume bridges the gap and introduces key biochemistry and inorganic concepts and also discusses recent developments. This is not an exhaustive research review, but a fantastic resource for an undergraduate special topics course. Roat-Malone has done a great job updating the content and including references as recent as 2006 in this second edition. Summing Up: Highly recommended. Upper-division undergraduates and graduate students. R. M. Granger II Sweet Briar College

Notas de autor provistas por Syndetics

Rosette M. Roat-Malone is Adjunct Professor of Chemistry at Washington College in Chestertown, Maryland.