Produkt

KlappentextWritten by a preeminent teacher and scientist in the field, this book provides specialists, students, and general readers with an understanding of the basic chemistry of interactions of inorganic substances with biological systems at the molecular level. The author presents bioinorganic concepts in context and brings a distinct chemistry perspective to the subject.
•Provides the streamlined coverage appropriate for one-semester courses or independent study, with all of the necessary but none of the excessive information
•Prepares readers to move to the next level of study (whether they continue on in the field or transition to medicine/industry)
•Presents concepts through extensive four-color visuals, appealing to a range of learning styles
•Promotes critical thinking through open-ended questions throughout the narrative and at the end of each chapter

Details

Weitere ISBN/GTIN9780080886978

ProduktartE-Book

EinbandartE-Book

FormatPDF

Format HinweisDRM Adobe

Verlag

Elsevier Science & Techn.

Erscheinungsjahr2010

Erscheinungsdatum20.07.2010

Seiten360 Seiten

SpracheEnglisch

IllustrationenApprox. 130 illustrations (50 in full color)

Artikel-Nr.2744479

Rubriken

Genre9200

Inhalt/Kritik

Inhaltsverzeichnis

1;Front Cover;1
2;Bioinorganic Chemistry: A Survey;4
3;Copyright Page;5
4;Contents;6
5;Preface;14
6;Introduction: Basics of Bio/Ecosystems and Biochemistry, and Other Basic Concepts;18
6.1;Biosphere (Ecosystem);18
6.1.1;Components of the Biosphere-Living Organisms;18
6.1.2;Bodily Structures of Living Organisms;20
6.2;Cells, the Basic Functional Units of Living Organisms;20
6.3;Biochemical Compounds Essential to Life;21
6.3.1;Carbohydrates;22
6.3.1.1;Monosaccharides;22
6.3.1.2;Polysaccharides and Derivatives;24
6.3.2;Lipids;25
6.3.2.1;Fats and Phospholipids;26
6.3.2.2;Steroids;27
6.3.3;Proteins and Amino Acids;27
6.3.3.1;Structures;27
6.3.3.2;Reactions-Formation and Hydrolysis of Protein;33
6.3.4;Vitamins (Coenzymes), Nucleotides, and Others;34
6.3.4.1;Coenzymes;34
6.3.4.2;Nucleotides;35
6.3.4.3;Other Vitamins;36
6.3.5;DNA/RNA (Polynucleotide);36
6.3.5.1;Structures;36
6.3.5.2;Reactions;40
6.4;Types of Biochemical Reactions;41
6.4.1;Reactions of Acid-Base Type;41
6.4.2;Reactions of Oxidation-Reduction Type;42
6.4.2.1;The Idea of Oxidation State;43
6.4.2.2;The Oxidation State of C in Organic Compounds and Recognition of Oxidation-Reduction Reactions;43
6.4.2.3;Other Kinds of Oxidation-Reduction Reactions;46
6.4.3;Free Radical Reactions;47
6.5;Transition State Theory of Reaction, and Enzyme Kinetics;47
6.5.1;Energy Profile and Transition State Theory of Reaction;48
6.5.2;Enzyme Kinetics;49
6.5.3;Enzyme Reaction Mechanism;50
7;CHAPTER 1 The Distribution of Elements;54
7.1;1.1. The Distribution of Elements in the Earth's Crust, Seawater, and Organisms;54
7.2;1.2. The Engines That Drive the Biochemical Cycling of the Elements;58
7.3;1.3. Flow of the Elements-Biogeochemical Cycling;59
7.4;1.4. Historical Change in the Biogeochemical Cycling of Elements;62
8;CHAPTER 2 Biological Needs for and the Behaviors of Inorganic Elements;70
8.1;2.1. Introduction;70
8.2;2.2. Inorganic Elements in the Biological Systems;71
8.2.1;2.2.1. Inorganic Elements Involved at the Molecular Level;71
8.2.2;2.2.2. Inorganic Elements Involved at the Cellular Level;72
8.2.3;2.2.3. Inorganic Elements Involved at the Physiological Level;72
8.2.4;2.2.4. Biological Systems Involved in the Metabolism of Inorganic Elements;73
8.3;2.3. Why Has a Specific Organism Chosen Specific Elements for Its Specific Needs?;75
8.4;2.4. Behaviors of Inorganic Elements-I: Fundamentals of Coordination Chemistry;75
8.4.1;2.4.1. Coordination Compounds or Metal Complexes;76
8.4.2;2.4.2. Ligand Field Theory-How the Predominant Structure Is Determined;77
8.4.3;2.4.3. Thermodynamic Tendency to Form Coordination Compounds;81
8.4.4;2.4.4. Chelate Effect;83
8.4.5;2.4.5. Ligand Substitution Reactions-Kinetic Factors;84
8.4.6;2.4.6. Oxidation-Reduction and Reduction Potential;85
8.5;2.5. Behaviors of Inorganic Elements-II: Basics of Organometallic Chemistry;90
8.5.1;2.5.1. Metal Carbonyls and the 18-Electron (18 e[sup(-)]) Rule;90
8.5.2;2.5.2. Other Organometallic Compounds;92
8.5.3;2.5.3. Some Special Types of Reactions Involving Organometallic Compounds;93
9;CHAPTER 3 How Do Enzymes Work?;98
9.1;3.1. Enzymatic Enhancement of Reaction Rate: General Considerations;98
9.1.1;3.1.1. Transition State Theory;99
9.1.2;3.1.2. The Dynamic Effects;102
9.1.3;3.1.3. A Composite Theory;104
9.2;3.2. Metalloenzymes/Proteins and Metal-Activated Enzymes;106
10;CHAPTER 4 Reactions of Acid-Base Type and the Functions of Metal Cations;110
10.1;4.1. General Considerations;110
10.1.1;4.1.1. Different Types (Definitions) of Acid-Base;110
10.1.2;4.1.2. Reactions of Acid-Base Type Catalyzed by Enzymes;111
10.1.3;4.1.3. Acidity Scale and Acid Character of Metal Cations: Prominence of Zn(II) and Mg(II);112
10.1.4;4.1.4. Kinetic Factors;115
10.1.5;4.1.5. Enhancement of Reaction by Protein Residues;116
10.2;4.2. Mg(II)-Dependent Enzymes;117
10.2.1;4.2.1. Rubisco (Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase);117
10.2.2;4.2.2. Pyruvate Kinase;118
10.3;4.3. Zn(II)-Dependent Enzymes;119
10.3.1;4.3.1. Carbonic Anhydrase;120
10.3.2;4.3.2. Thermolysin, Carboxypeptidase A, and Others;122
10.3.3;4.3.3. Leucine Aminopeptidase;123
10.3.4;4.3.4. Alkaline Phosphatase and Purple Acid Phosphatase;123
10.3.5;4.3.5. Alcohol Dehydrogenase;124
10.4;4.4. Other Metal Cation-Dependent Acid-Base Enzymes;125
10.4.1;4.4.1. Aconitase, an Iron-Sulfur Enzyme, and Others;125
10.4.2;4.4.2. Arginase: Mn Enzyme;126
10.4.3;4.4.3. Urease and Other Ni Enzymes;126
10.5;4.5. Structural Effects of Metal Ions;128
10.6;4.6. Metal Ions and Polynucleic Acids (DNA and RNA);129
10.6.1;4.6.1. General Characteristics of Interactions of Metal Ions with Polynucleotides;130
10.6.1.1;4.6.1.1. Effects on Structures;130
10.6.1.2;4.6.1.2. Catalytic Metal Ions in DNA Polymerases and Nucleases;131
10.6.2;4.6.2. Gene Regulation and Metal Ions;133
10.6.3;4.6.3. Ribozymes;134
11;CHAPTER 5 Reactions of Oxidation-Reduction Type Including Electron Transfer Processes;140
11.1;5.1. General Consideration;140
11.1.1;5.1.1. Reduction Potential;141
11.1.1.1;5.1.1.1. Heme Proteins and Enzymes;141
11.1.1.2;5.1.1.2. Iron-Sulfur Proteins;144
11.1.1.3;5.1.1.3. Copper Proteins;147
11.1.1.4;5.1.1.4. Molybdenum and Tungsten Proteins;148
11.1.2;5.1.2. Kinetic Factors-Electron Transfer between and in Protein(s);149
11.2;5.2. Iron Enzymes and Proteins;150
11.2.1;5.2.1. Cytochromes and Iron-Sulfur Electron Transfer Proteins;151
11.2.2;5.2.2. Nitrite Reductase and Nitric Oxide Reductase;151
11.2.3;5.2.3. Horseradish Peroxidase (HRP), Catalase, and Cytochrome C Peroxidase;152
11.2.4;5.2.4. Hydrogenase;154
11.3;5.3. Copper Enzymes and Proteins;154
11.3.1;5.3.1. Blue Copper Proteins;155
11.3.2;5.3.2. Blue Copper Oxidases;156
11.3.3;5.3.3. Cytochrome C Oxidase;157
11.3.4;5.3.4. Nitrite Reductase and Nitrous Oxide Reductase;157
11.3.5;5.3.5. Amine Oxidases;159
11.3.6;5.3.6. Superoxide Dismutase (SOD);161
11.4;5.4. Molybdenum Enzymes and Tungsten Enzymes;162
11.4.1;5.4.1. Xanthine Oxidase and Aldehyde Oxidase;162
11.4.2;5.4.2. Sulfite Oxidase and Nitrate Reductase (Assimilatory);164
11.4.3;5.4.3. DMSO Reductase and Nitrate Reductase (Respiratory or Dissimilatory);165
11.4.4;5.4.4. Tungsten Enzymes;167
11.5;5.5. Manganese Oxidoreductases;167
11.5.1;5.5.1. Manganese Catalase;168
11.5.2;5.5.2. Water Oxidase;168
11.6;5.6. Ni-Containing Redox Enzymes;170
11.6.1;5.6.1. Ni-Fe (Se) Hydrogenase;171
11.6.2;5.6.2. Carbon Monoxide Dehydrogenase (CODH);172
11.6.3;5.6.3. Acetyl CoA Synthase (ACS);173
11.6.4;5.6.4. Methyl-Coenzyme M Reductase;173
12;CHAPTER 6 Oxygen Carrying Processes and Oxygenation Reactions;178
12.1;6.1. The Chemistry of Oxygen, Dioxygen, and Related Entities;178
12.1.1;6.1.1. Electronic Structures;178
12.1.2;6.1.2. Basic Reactions of O and O[sub(2)];179
12.1.3;6.1.3. Reactions of Ground State O and O[sub(2)];180
12.1.4;6.1.4. Interactions of Ground State O[sub(2)] with Compounds of Transition Metals;181
12.1.5;6.1.5. Reactions of Oxygen Derivatives;184
12.2;6.2. Reversible O[sub(2)] Binding: Oxygen Carriers;185
12.3;6.3. Monooxygenases;186
12.3.1;6.3.1. Monooxygenases Dependent on Cytochrome P-450;187
12.3.2;6.3.2. Nonheme Mononuclear Iron Monooxygenases;190
12.3.3;6.3.3. Nonheme Dinuclear Iron Monooxygenases;193
12.3.4;6.3.4. Copper Monooxygenases;194
12.4;6.4. Dioxygenases;195
12.5;6.5. Prostaglandin Endoperoxide Synthase;198
13;CHAPTER 7 Metal-Involving Free Radical Reactions;202
13.1;7.1. A Survey of Biologically Relevant Free Radicals;202
13.2;7.2. Why Radicals?;204
13.3;7.3. Reactivities of Free Radicals;205
13.4;7.4. B[sub(12)]-Coenzyme (Adenosylcobalamin)-Dependent Enzymes;209
13.4.1;7.4.1. Mutases, Diol Dehydratase, and Ethanolamine Ammonia Lyase;209
13.4.1.1;7.4.1.1. Homolytic Cleavage of the Cobalt-to-Carbon Bond upon Binding a Substrate;210
13.4.1.2;7.4.1.2. Hydrogen Abstraction from Substrates;212
13.4.1.3;7.4.1.3. 1,2-Shift or Other Reactions of Substrate Free Radicals;212
13.4.2;7.4.2. Ribonucleotide Reductases (Cobalamin-Dependent);215
13.5;7.5. S-Adenosyl Methionine (SAM)-Dependent Enzymes;216
13.6;7.6. Iron-Dependent Ribonucleotide Reductases;217
13.7;7.7. Galactose Oxidase;219
13.8;7.8. Other Examples;220
14;CHAPTER 8 Nitrogen Fixation;222
14.1;8.1. Nitrogen Metabolism;222
14.2;8.2. Chemistry of N[sub(2)] Reduction;223
14.3;8.3. Mo-Dependent Nitrogenase;225
14.4;8.4. Other Nitrogenases;231
15;CHAPTER 9 Other Essential Elements;234
15.1;9.1. Introduction;234
15.2;9.2. Biochemistry of Nitrogen Compounds;235
15.3;9.3. Biochemistry of Phosphorus;236
15.4;9.4. Biochemistry of Sulfur Compounds;236
15.4.1;9.4.1. Cellular Processes;236
15.4.2;9.4.2. Marine Biogeochemical Cycling;238
15.5;9.5. Selenium;239
15.5.1;9.5.1. Chemistry of Selenium as Compared to That of Sulfur;239
15.5.2;9.5.2. Glutathione and Selenium: Glutathione Peroxidase;239
15.5.3;9.5.3. Thioredoxin Reductase;241
15.5.4;9.5.4. Other Selenium-Containing Proteins and Enzymes;242
15.6;9.6. Boron;242
15.7;9.7. Silicon;244
15.7.1;9.7.1. Chemistry of Silicon;245
15.7.2;9.7.2. Frustules of Diatoms;246
15.7.3;9.7.3. Spicules in Sponge;247
15.7.4;9.7.4. Other Biological Functions of Silicon;248
15.8;9.8. Vanadium;249
15.8.1;9.8.1. Vanabins;249
15.8.2;9.8.2. Amavadin;250
15.8.3;9.8.3. Haloperoxidases;250
15.9;9.9. Chromium;252
15.10;9.10. Halogens and the Like;252
15.10.1;9.10.1. Formation of Volatile Halocarbons in Macroalgae;253
15.10.2;9.10.2. HOX Formation in Mammals and Others;253
15.10.2.1;9.10.2.1. Formation of HOX by a Fungal Chloroperoxidase;253
15.10.2.2;9.10.2.2. Formation of HOX by Mammalian Peroxidases;254
16;CHAPTER 10 Metal-Related Physiology;260
16.1;10.1. Metabolism of Metallic Elements;261
16.1.1;10.1.1. Iron Metabolism (in Mammals);261
16.1.1.1;10.1.1.1. Ferric Reductase;262
16.1.1.2;10.1.1.2. Divalent Metal Transporter (DMT1);263
16.1.1.3;10.1.1.3. Ferroxidase;263
16.1.1.4;10.1.1.4. Transferrin (Tf) and Transferrin Receptor (TfR);263
16.1.1.5;10.1.1.5. Ferritin;265
16.1.1.6;10.1.1.6. Ferroportin (Fpn)/Hepcidin;266
16.1.1.7;10.1.1.7. Regulation of Ferritin and Transferrin;266
16.1.1.8;10.1.1.8. Iron Metabolism in Bacteria, Fungi, and Plants;267
16.1.2;10.1.2. Copper Metabolism;269
16.1.2.1;10.1.2.1. Outline of Copper Metabolism in Mammals;269
16.1.2.2;10.1.2.2. Copper Metabolism in Bacteria and Plants;270
16.1.3;10.1.3. Zinc Metabolism;271
16.1.3.1;10.1.3.1. In Mammals;271
16.1.3.2;10.1.3.2. In E. coli;272
16.1.4;10.1.4. A Mg(II) Transporter;273
16.2;10.2. Physiological Roles Played by Metallic Elements;273
16.2.1;10.2.1. Na/K-ATPase and Ca-ATPase;273
16.2.1.1;10.2.1.1. Mechanism;273
16.2.1.2;10.2.1.2. Ion Selectivity in Metal Ion Transporters and Channels-A General Discussion;274
16.2.2;10.2.2. Ca(II)-Second Messenger and Other Functions;276
16.2.2.1;10.2.2.1. Control of Cytoplasmic Ca(II) Concentration;277
16.2.2.2;10.2.2.2. Basic Mechanisms of Ca(II)-Physiology;278
16.2.2.3;10.2.2.3. Synaptotagmin, an Example of Physiology Mediated by Ca(II);279
16.2.2.4;10.2.2.4. Why Calcium(II)?;280
16.2.3;10.2.3. Zinc-Enriched Neuron (ZEN);283
16.2.4;10.2.4. Sensors for Small Molecules;283
16.2.4.1;10.2.4.1. Oxygen Sensors;284
16.2.4.2;10.2.4.2. CO-Sensors;285
16.2.4.3;10.2.4.3. NO-Sensors;286
16.2.4.4;10.2.4.4. H[sub(2)]-Sensors;287
16.2.4.5;10.2.4.5. Redox Sensors;287
16.2.5;10.2.5. Plant Hormone Ethylene and Copper;288
16.2.6;10.2.6. Magnetic Navigation;288
16.2.7;10.2.7. Radiation Shields;289
16.3;10.3. Biological Skeletons (Biominerals);289
16.3.1;10.3.1. Calcium Carbonate;290
16.3.2;10.3.2. Calcium Oxalate;292
16.3.3;10.3.3. Calcium Phosphate;292
17;CHAPTER 11 Environmental Bioinorganic Chemistry;296
17.1;11.1. General Considerations;296
17.2;11.2. Toxicity of Inorganic Compounds;298
17.2.1;11.2.1. Abundance and Toxicity;298
17.2.2;11.2.2. Toxicity of Reactive Oxygen Species, and Defense Mechanisms Against Them;299
17.3;11.3. Molecular Mechanisms of Toxicity of Inorganic Compounds;301
17.3.1;11.3.1. Discrimination of Elements by Organisms-General Considerations;301
17.3.2;11.3.2. Oxidative Stress and Metals and As-General Effects;305
17.3.3;11.3.3. Individual Element's (Acute) Toxicity;307
17.3.3.1;11.3.3.1. Cd(II) and Hg(II);307
17.3.3.2;11.3.3.2. Pb(II);307
17.3.3.3;11.3.3.3. Organometallic Compounds;308
17.3.3.4;11.3.3.4. Organotin Compounds;309
17.3.3.5;11.3.3.5. Be(II), Al(III);309
17.3.3.6;11.3.3.6. Tl(I);310
17.3.3.7;11.3.3.7. Cr;310
17.3.3.8;11.3.3.8. Ni(II);310
17.3.3.9;11.3.3.9. Anions;311
17.3.4;11.3.4. Alzheimer's Disease and Metals;311
17.4;11.4. Biological Defenses against Toxicity;312
17.4.1;11.4.1. Biological Defense against Mercury;313
17.4.2;11.4.2. Metallothioneins and Phytochelatins;315
17.4.2.1;11.4.2.1. Metallothioneins;315
17.4.2.2;11.4.2.2. Copper-Thionein (Cu-MT);316
17.4.2.3;11.4.2.3. Phytochelatins;317
17.4.2.4;11.4.2.4. Use of Sulfide;318
17.4.3;11.4.3. Defense against Lead;318
17.4.4;11.4.4. Biotransformation of Arsenic;319
17.5;11.5. Bioremediaion of Metals;320
17.5.1;11.5.1. Biosorption by Brown Algae and by Microbial Surfactants;320
17.5.2;11.5.2. Phytoremediation (Phytoextraction of Metals from Soil);322
17.5.3;11.5.3. Phytoextraction by Microalgae (Remediation of Polluted Water);325
17.5.4;11.5.4. Other Types of Bioremediation;325
18;CHAPTER 12 Medical Applications of Inorganic Compounds: Medicinal Inorganic Chemistry;328
18.1;12.1. Introduction;328
18.2;12.2. Cancer Therapy;329
18.2.1;12.2.1. Platinum Compounds;330
18.2.2;12.2.2. Bleomycin;333
18.2.3;12.2.3. Radioactive Pharmaceuticals;336
18.3;12.3. Gold Compounds for Rheumatoid Arthritis;336
18.4;12.4. Vanadium Compounds for Diabetes;337
18.5;12.5. Lithium Compounds for Psychiatric Disorders;339
18.6;12.6. Other Potential Drugs Containing Inorganic Compounds;340
18.7;12.7. Diagnostic (Imaging) Agents;340
18.7.1;12.7.1. Gd(III)-Contrasting Agents for MRI;340
18.7.2;12.7.2. [sub(99m)]Tc-Radioactive Diagnostic Pharmaceuticals;341
19;Appendix;344
20;References;346
21;Index;368
21.1;A;368
21.2;B;368
21.3;C;368
21.4;D;369
21.5;E;369
21.6;F;369
21.7;G;370
21.8;H;370
21.9;I;370
21.10;K;370
21.11;L;370
21.12;M;370
21.13;N;371
21.14;O;371
21.15;P;371
21.16;Q;372
21.17;R;372
21.18;S;372
21.19;T;372
21.20;U;372
21.21;V;373
21.22;W;373
21.23;X;373
21.24;Y;373
21.25;Z;373mehr

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Bioinorganic Chemistry

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Química bioinorgánica

Chemicals for Life and Living

General Principles of Biochemistry of the Elements

General Principles of Biochemistry of the Elements

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