Bioinorganic Chemistry
Автор(ы): | Roat-Malone M. Rosette
06.10.2007
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Год изд.: | 2002 |
Описание: | Bioinorganic chemical knowledge grows more interesting and more complex with each passing year. As more details about the usage and utility of metals in biological species and more mechanistic and structural information becomes available about bioinorganic molecules, more biologists, chemists, and physicists will become interested in the field. Senior-level undergraduates in chemistry, biology, and physics, as well as beginning graduate students, will do well to educate themselves in this diverse and fascinating chemical area. |
Оглавление: |
Обложка книги.
1 Inorganic Chemistry Essentials [1]1.1 Introduction [1] 1.2 Essential Chemical Elements [1] 1.3 Metals in Biological Systems: A Survey [3] 1.4 Inorganic Chemistry Basics [6] 1.5 Biological Metal Ion Complexation [7] 1.5.1 Thermodynamics [7] 1.5.2 Kinetics [8] 1.6 Electronic and Geometric Structures of Metals in Biological Systems [11] 1.7 Bioorganometallic Chemistry [16] 1.8 Electron Transfer [19] 1.9 Conclusions [22] References [22] 2 Biochemistry Fundamentals [24] 2.1 Introduction [24] 2.2 Proteins [25] 2.2.1 Amino Acid Building Blocks [25] 2.2.2 Protein Structure [27] 2.2.3 Protein Sequencing and Proteomics [33] 2.2.4 Protein Function, Enzymes, and Enzyme Kinetics [36] 2.3 Nucleic Acids [39] 2.3.1 DNA and RNA Building Blocks [39] 2.3.2 DNA and RNA Molecular Structures [42] 2.3.3 Transmission of Genetic Information [46] 2.3.4 Genetic Mutations and Site-Directed Mutagenesis [48] 2.3.5 Genes and Cloning [50] 2.3.6 Genomics and the Human Genome [52] 2.4 Zinc-Finger Proteins [54] 2.4.1 Descriptive Examples [57] 2.5 Conclusions [63] References [63] 3 Instrumental and Computer-Based Methods [66] 3.1 Introduction [66] 3.1.1 Analytical Instrument-Based Methods [66] 3.1.2 Spectroscopy [67] 3.2 X-Ray Absorption Spectroscopy (XAS) and Extended X-Ray Absorption Fine Structure (EXAFS) [68] 3.2.1 Theoretical Aspects and Hardware [68] 3.2.2 Descriptive Examples [70] 3.3 X-Ray Crystallography [73] 3.3.1 Introduction [73] 3.3.2 Crystallization and Crystal Habits [74] 3.3.3 Theory and Hardware [78] 3.3.4 Descriptive Examples [83] 3.4 Electron Paramagnetic Resonance [85] 3.4.1 Theory and Determination of g-Values [85] 3.4.2 Hyperfme and Superhyperfme Interactions [91] 3.4.3 Descriptive Examples [91] 3.5 Nuclear Magnetic Resonance [93] 3.5.1 Theoretical Aspects [93] 3.5.2 Nuclear Screening and the Chemical Shift [98] 3.5.3 Spin-Spin Coupling [101] 3.5.4 Techniques of Spectral Integration and Spin-Spin Decoupling [103] 3.5.5 Nuclear Magnetic Relaxation [103] 3.5.6 The Nuclear Overhauser Effect (NOE) [104] 3.5.7 Obtaining the NMR Spectrum [106] 3.5.8 Two-Dimensional (2D) NMR Spectroscopy [107] 3.5.9 Two-Dimensional Correlation Spectroscopy (COSY) [108] 3.5.10 Nuclear Overhauser Effect Spectroscopy (NOESY) [110] 3.5.11 Descriptive Examples [111] 3.6 Mossbauer Spectroscopy [114] 3.6.1 Theoretical Aspects [114] 3.6.2 Quadrupole Splitting and the Isomer Shift [116] 3.6.3 Magnetic Hyperfine Interactions [117] 3.6.4 Descriptive Examples [119] 3.7 Other Instrumental Methods [121] 3.7.1 Atomic Force Microscopy [121] 3.7.2 Fast and Time-Resolved Methods [123] 3.7.2.1 Stopped-Flow Kinetic Methods [123] 3.7.2.2 Hash Photolysis [124] 3.7.2.3 Time-Resolved Crystallography [124] 3.8 Introduction to Computer-Based Methods [126] 3.9 Computer Hardware [126] 3.10 Molecular Modeling and Molecular Mechanics [129] 3.10.1 Introduction to MM [129] 3.10.2 Molecular Modeling, Molecular Mechanics, and Molecular Dynamics [130] 3.10.3 Biomolecule Modeling [134] 3.10.4 Molecular Modeling Descriptive Examples [135] 3.11 Quantum Mechanics-Based Computational Methods [138] 3.11.1 Introduction [138] 3.11.2 Ab-Initio Methods [138] 3.11.3 Density Function Theory [139] 3.11.4 Semiempirical Methods [140] 3.12 Computer Software for Chemistry [141] 3.12.1 Mathematical Software [148] 3.13 World Wide Web Online Resources [149] 3.13.1 Nomenclature and Visualization Resources [149] 3.13.2 Online Societies, Literature, Materials, Equipment Web Servers [151] 3.14 Summary and Conclusions [153] References [153] 4 Iron-Containing Oxygen Carriers and Their Synthetic Models [158] 4.1 Introduction [158] 4.2 Myoglobin and Hemoglobin Basics [163] 4.3 Structure of the Prosthetic Group [165] 4.4 Analytical Techniques [166] 4.5 Mechanism for Reversible Binding of Dioxygen and Cooperativity of Oxygen Binding [168] 4.6 Behavior of Dioxygen Bound to Metals [171] 4.7 Structure of the Active Site in Myoglobin and Hemoglobin: Comparison to Model Compounds [172] 4.8 Model Compounds [176] 4.8.1 Cobalt-Containing Model Compounds [176] 4.8.2 Iron-Containing Model Compounds [177] 4.9. Binding of CO to Myoglobin, Hemoglobin, and Model Compounds [182] 4.10. Conclusions [184] References [185] 5 Copper Enzymes [187] 5.1 Introduction, Occurrence, Structure, Function [187] 5.2 Discussion of Specific Enzymes [193] 5.2.1 Azurin [193] 5.2.2 Plastocyanin [197] 5.2.3 Superoxide Dismutase [199] 5.2.4 Hemocyanin [209] 5.3 Model Compounds [214] 5.3.1 Introduction [214] 5.3.2 Type I Copper Enzyme Models [215] 5.3.3 Type II Copper Enzyme Models [216] 5.3.4 Type III Copper Enzyme Models [217] 5.3.4.1 Karlin Group Tridentate Model Compounds [217] 5.3.4.2 Tolman Group Tetradentate Model Compounds [221] 5.3.4.3 Kitajima Group Tetradentate Model Compounds [222] 5.3.4.4 Karlin Group Tetradentate Model Compounds [226] 5.3.5 Summary [227] 5.4 Conclusions [228] References [228] 6 The Enzyme Nitrogenase [231] 6.1 Introduction [231] 6.2 Detailed Mechanistic Studies [235] 6.3 Iron-Sulfur Clusters [239] 6.4 Fe-Protein Structure [241] 6.5 MoFe-Protein Structure [244] 6.5.1 Overview [244] 6.5.2 Details of the P-Cluster [247] 6.5.3 Details of the M Center [251] 6.6 Nitrogenase Model Compounds [254] 6.6.1 Structural Models [255] 6.6.2 Functional Models [258] 6.7 Conclusions [261] References [262] 7 Metals in Medicine [265] 7.1 Introduction [265] 7.1.1 Inorganic Medicinal Chemistry [265] 7.1.2 Metal Toxicity and Homeostasis [266] 7.2 Therapeutic Compounds [269] 7.2.1 Superoxide Dismutase Mimics [269] 7.2.2 Vanadium-Based Diabetes Drugs [273] 7.2.2.1 Introduction [273] 7.2.2.2 Examples of Vanadium Compounds Tested as Insulin Mimetic Agents [275] 7.2.2.3 The Role of Chromium [278] 7.2.3 Platinum-Containing Anticancer Agents [279] 7.2.3.1 Cis- and frans-Dichlorodiammineplatinum(II) [279] 7.2.3.2 Mechanism of cisDDP Antitumor Activity [281] 7.2.3.3 Drug Resistance and DNA Repair Mechanisms [286] 7.2.3.4 A New Nonclassical Platinum Antitumor Agent [288] 7.2.3.5 Other Platinum-Containing Anticancer Compounds [290] 7.2.3.6 Conclusions [292] 7.3 Diagnostic Agents [292] 7.3.1 Technetium Imaging Agents [292] 7.3.1.1 Introduction [292] 7.3.1.2 "Technetium Essential" Radiopharmaceuticals [294] 7.3.1.3 "Technetium Tagged" Radiopharmaceuticals [295] 7.3.2 Gadolinium MRI Imaging Agents [300] 7.3.2.1 Introduction [300] 7.3.2.2 Magnetic Imaging Considerations, Kinetics, and Thermodynamics of Complexes [301] 7.3.2.3 Selected Drugs in Usage or in Trials [304] 7.4 Metal Transport and Metallochaperones [312] 7.4.1 Introduction [312] 7.4.2 The Atxl Metallochaperone [314] 7.4.3 Hahl or Atoxl Metallochaperone [316] 7.4.4 Superoxide Dismutase Metallochaperones [317] 7.4.5 Copper Toxicity, Disease States, and Treatments [319] 7.4.5.1 Familial Amyotrophic Lateral Sclerosis (FALS) [319] 7.4.5.2 Wilson and Menkes Diseases [321] 7.4.6 Conclusions [324] 7.5 Metals in Medicine (MIM) [325] 7.5.1 Summary, Goals; Past, Present, and Future MIM Development [325] References [329] Index [337] |
Формат: | djvu |
Размер: | 4347304 байт |
Язык: | ENG |
Рейтинг: | 86 |
Открыть: | Ссылка (RU) |