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Cover image for Bioinorganic chemistry : a short course
Title:
Bioinorganic chemistry : a short course
Publication Information:
Hoboken, NJ : John Wiley & Sons, 2007
ISBN:
9780471761136
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30000010161121 QP531 R62 2008 Open Access Book Book
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Summary

Summary

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.


Author Notes

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


Reviews 1

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


Table of Contents

Prefacep. xiii
Acknowledgmentsp. xix
1 Inorganic Chemistry Essentialsp. 1
1.1 Introductionp. 1
1.2 Essential Chemical Elementsp. 1
1.3 Metals in Biological Systems: A Surveyp. 3
1.4 Inorganic Chemistry Basicsp. 6
1.5 Biological Metal Ion Complexationp. 8
1.5.1 Thermodynamicsp. 8
1.5.2 Kineticsp. 9
1.6 Electronic and Geometric Structures of Metals in Biological Systemsp. 13
1.7 Bioorganometallic Chemistryp. 19
1.8 Electron Transferp. 22
1.9 Conclusionsp. 26
Referencesp. 27
2 Biochemistry Fundamentalsp. 29
2.1 Introductionp. 29
2.2 Proteinsp. 30
2.2.1 Amino Acid Building Blocksp. 30
2.2.2 Protein Structurep. 33
2.2.3 Protein Sequencing and Proteomicsp. 39
2.2.4 Protein Function, Enzymes, and Enzyme Kineticsp. 43
2.3 Nucleic Acidsp. 47
2.3.1 DNA and RNA Building Blocksp. 47
2.3.2 DNA and RNA Molecular Structuresp. 47
2.3.3 Transmission of Genetic Informationp. 53
2.3.4 Genetic Mutations and Site-Directed Mutagenesisp. 56
2.3.5 Genes and Cloningp. 58
2.3.6 Genomics and the Human Genomep. 61
2.4 Zinc-Finger Proteinsp. 63
2.4.1 Descriptive Examplesp. 67
2.5 Summary and Conclusionsp. 73
Referencesp. 74
3 Instrumental Methodsp. 76
3.1 Introductionp. 76
3.1.1 Analytical Instrument-Based Methodsp. 76
3.1.2 Spectroscopyp. 77
3.2 X-Ray Absorption Spectroscopy (XAS) and Extended X-Ray Absorption Fine Structure (EXAFS)p. 78
3.2.1 Theoretical Aspects and Hardwarep. 78
3.2.2 Descriptive Examplesp. 81
3.3 X-Ray Crystallographyp. 83
3.3.1 Introductionp. 83
3.3.2 Crystallization and Crystal Habitsp. 84
3.3.3 Theory and Hardwarep. 88
3.3.4 Descriptive Examplesp. 95
3.4 Nuclear Magnetic Resonancep. 98
3.4.1 Theoretical Aspectsp. 98
3.4.2 Nuclear Screening and the Chemical Shiftp. 101
3.4.3 Spin-Spin Couplingp. 104
3.4.4 Techniques of Spectral Integration and Spin-Spin Decouplingp. 106
3.4.5 Nuclear Magnetic Relaxationp. 107
3.4.6 The Nuclear Overhauser Effect (NOE)p. 108
3.4.7 Obtaining the NMR Spectrump. 110
3.4.8 Two-Dimensional (2D) NMR Spectroscopyp. 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 NMRp. 116
3.4.12 Descriptive Examplesp. 117
3.5 Electron Paramagnetic Resonancep. 122
3.5.1 Theory and Determination of g-Valuesp. 122
3.5.2 Hyperfine and Superhyperfine Interactionsp. 127
3.5.3 Electron Nuclear Double Resonance (ENDOR) and Electron Spin-Echo Envelope Modulation (ESEEM)p. 129
3.5.4 Descriptive Examplesp. 129
3.6 Mossbauer Spectroscopyp. 132
3.6.1 Theoretical Aspectsp. 132
3.6.2 Quadrupole Splitting and the Isomer Shiftp. 134
3.6.3 Magnetic Hyperfine Interactionsp. 136
3.6.4 Descriptive Examplesp. 137
3.7 Other Instrumental Methodsp. 139
3.7.1 Atomic Force Microscopyp. 139
3.7.2 Fast and Time-Resolved Methodsp. 143
3.7.2.1 Stopped-Flow Kinetic Methodsp. 143
3.7.2.2 Flash Photolysisp. 144
3.7.2.3 Time-Resolved Crystallographyp. 146
3.7.3 Mass Spectrometryp. 148
3.8 Summary and Conclusionsp. 153
Referencesp. 154
4 Computer Hardware, Software, and Computational Chemistry Methodsp. 157
4.1 Introduction to Computer-Based Methodsp. 157
4.2 Computer Hardwarep. 157
4.3 Molecular Modeling and Molecular Mechanicsp. 160
4.3.1 Introduction to MMp. 160
4.3.2 Molecular Modeling, Molecular Mechanics, and Molecular Dynamicsp. 161
4.3.3 Biomolecule Modelingp. 166
4.3.4 A Molecular Modeling Descriptive Examplep. 167
4.4 Quantum Mechanics-Based Computational Methodsp. 170
4.4.1 Introductionp. 170
4.4.2 Ab Initio Methodsp. 170
4.4.3 Density Function Theoryp. 171
4.4.4 Semiempirical Methodsp. 173
4.5 Computer Software for Chemistryp. 174
4.5.1 Mathematical Softwarep. 180
4.6 World Wide Web Online Resourcesp. 181
4.6.1 Nomenclature and Visualization Resourcesp. 181
4.6.2 Online Societies, Online Literature Searching, and Materials and Equipment Websitesp. 183
4.7 Summary and Conclusionsp. 185
Referencesp. 185
5 Group I and II Metals in Biological Systems: Homeostasis and Group I Biomoleculesp. 189
5.1 Introductionp. 189
5.2 Homeostasis of Metals (and Some Nonmetals)p. 192
5.2.1 Phosphorus as Phosphatep. 192
5.2.2 Potassium, Sodium, and Chloride Ionsp. 193
5.2.3 Calcium Homeostasisp. 194
5.3 Movement of Molecules and Ions Across Membranesp. 195
5.3.1 Passive Diffusionp. 195
5.3.2 Facilitated Diffusionp. 197
5.3.2.1 Gated Channelsp. 197
5.3.3 Active Transport-Ion Pumpsp. 197
5.4 Potassium-Dependent Moleculesp. 199
5.4.1 Na[superscript +]/K[superscript +] ATPase: The Sodium Pumpp. 199
5.4.2 Potassium (K[superscript +]) Ion Channelsp. 203
5.4.2.1 Introductionp. 203
5.4.2.2 X-Ray Crystallographic Studiesp. 205
5.5 Conclusionsp. 235
Referencesp. 235
6 Group I and II Metals in Biological Systems: Group IIp. 238
6.1 Introductionp. 238
6.2 Magnesium and Catalytic RNAp. 238
6.2.1 Introductionp. 238
6.2.2 Analyzing the Role of the Metal Ionp. 241
6.2.3 The Group I Intron Ribozymep. 244
6.2.4 The Hammerhead Ribozymep. 261
6.3 Calcium-Dependent Moleculesp. 301
6.3.1 Introductionp. 301
6.3.2 Calmodulinp. 302
6.3.2.1 Introductionp. 302
6.3.2.2 Calmodulin Structure by X-Ray and NMRp. 303
6.3.2.3 Calmodulin Interactions with Drug Moleculesp. 308
6.3.2.4 Calmodulin-Peptide Bindingp. 313
6.3.2.5 Conclusionsp. 326
6.4 Phosphoryl Transfer: P-Type ATPasesp. 327
6.4.1 Introductionp. 327
6.4.2 Calcium P-Type ATPasesp. 327
6.4.2.1 Ca[superscript 2+]-ATPase Protein SERCA1a and the Ca[superscript 2+]-ATPase Cyclep. 329
6.5 Conclusionsp. 337
Referencesp. 338
7 Iron-Containing Proteins and Enzymesp. 343
7.1 Introduction: Iron-Containing Proteins with Porphyrin Ligand Systemsp. 343
7.2 Myoglobin and Hemoglobinp. 343
7.2.1 Myoglobin and Hemoglobin Basicsp. 345
7.2.2 Structure of the Heme Prosthetic Groupp. 347
7.2.3 Behavior of Dioxygen Bound to Metalsp. 348
7.2.4 Structure of the Active Site in Myoglobin and Hemoglobin: Comparison to Model Compoundsp. 349
7.2.5 Some Notes on Model Compoundsp. 352
7.2.6 Iron-Containing Model Compoundsp. 353
7.2.7 Binding of CO to Myoglobin, Hemoglobin, and Model Compoundsp. 356
7.2.8 Conclusionsp. 359
7.3 Introduction to Cytochromesp. 359
7.4 Cytochrome P450: A Monooxygenasep. 361
7.4.1 Introductionp. 361
7.4.2 Cytochrome P450: Structure and Functionp. 363
7.4.3 Cytochrome P450: Mechanism of Activityp. 365
7.4.4 Analytical Methods: X-Ray Crystallographyp. 369
7.4.5 Cytochrome P450 Model Compoundsp. 372
7.4.5.1 Introductionp. 372
7.4.5.2 A Cytochrome P450 Model Compound: Structuralp. 372
7.4.5.3 Cytochrome P450 Model Compounds: Functionalp. 374
7.4.6 Cytochrome P450 Conclusionsp. 382
7.5 Cytochrome b(6)f: A Green Plant Cytochromep. 382
7.5.1 Introductionp. 382
7.5.2 Cytochrome b(6)f Metal Cofactor Specificsp. 386
7.6 Cytochrome bc[subscript 1]: A Bacterial Cytochromep. 388
7.6.1 Introductionp. 388
7.6.2 Cytochrome bc[subscript 1] Structurep. 389
7.6.3 Cytochrome bc[subscript 1] Metal Cofactor Specificsp. 391
7.6.4 The Cytochrome bc[subscript 1] Q Cyclep. 395
7.6.5 Cytochrome bc[subscript 1] Inhibitorsp. 397
7.6.6 Cytochrome bc[subscript 1] Conclusionsp. 408
7.7 Cytochromes cp. 408
7.7.1 Introductionp. 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 Apoptosisp. 422
7.7.4.1 Cytochrome c Foldingp. 422
7.7.4.2 Electron Transfer in Cytochrome c and Its Redox Partnersp. 424
7.7.4.3 Apoptosisp. 427
7.7.5 Cytochrome c Conclusionsp. 429
7.8 Cytochrome c Oxidasep. 429
7.8.1 Introductionp. 429
7.8.2 Metal-Binding Sites in Cytochrome c Oxidasep. 432
7.8.3 Dioxygen Binding, Proton Translocation, and Electron Transportp. 434
7.8.4 Cytochrome c Oxidase Model Compounds and Associated Analytical Techniquesp. 440
7.8.5 Cytochrome c Oxidase Conclusionsp. 453
7.9 Non-Heme Iron-Containing Proteinsp. 454
7.9.1 Introductionp. 454
7.9.2 Proteins with Iron-Sulfur Clustersp. 454
7.9.2.1 The Enzyme Aconitasep. 455
7.9.3 Iron-Oxo Proteinsp. 458
7.9.3.1 Methane Monooxygenasesp. 459
7.10 Conclusionsp. 465
Referencesp. 466
Indexp. 477
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