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Written by a preeminent teacher and scientist in the field, Bioinorganic Chemistry 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
Lecturers and students studying bioinorganic chemistry in inorganic, natural-products chemistry, and biochemistry programs *
Chapt. 0. Basics of Bio/ecosystems and Biochemistry, and Other Basic Concepts 0.1.Biosphere (Ecosystem) 0.1.1. Components of the biosphere-Living organisms 0.1.2. Bodily structure of living organisms 0.2. Cells, the Basic Functional Units of Living Organisms 0.3. Basic Biochemicals Essential to Life 0.3.1. Carbohydrates 0.3.1.1. Monosasccharides 0.3.1.2. Polysaccharides and derivatives 0.3.2. Lipids 0.3.2.1. Fats and phospholipids 0.3.2.2. Steroids 0.3.3. Proteins and amino acids 0.3.3.1. Structures 0.3.3.2. Reactions – formation and hydrolysis of protein 0.3.4. Nucleotides, vitamins (coenzymes) and others 0.3.4.1. Coenzymes 0.3.4.2. Nucleotides 0.3.4.3. Other vitamins 0.3.4.4. Hormone, neurotransmitters and others 0.3.5. DNA/RNA (Polynucleotide) 0.3.5.1. Structures 0.3.5.2. Reactions 0.4. Types of Biochemical Reactions 0.4.1. Reactions of acid-base type 0.4.2. Reactions of oxidation-reduction type 0.4.2.1. The idea of oxidation state 0.4.2.2. The oxidation state of “C” in organic compounds and recognition of oxidation-reduction reactions 0.4.2.3. Other kinds of oxidation-reduction reactions 0.4.3. Free radical reactions 0.5. Transition State Theory of Reaction, and Enzyme Kinetics 0.5.1. Energy profile and transition state theory of reaction 0.5.2. Enzyme Kinetics 0.5.3. Enzyme reaction mechanism
Chapt. 1. Distribution of Elements 1.1. Distribution of Elements in Earth Crust/Sea Water/Organisms 1.2. The Engines to Drive the Biochemical Cycling of the Elements 1.3. The Geochemical Cycling of Elements – Contribution by Biosphere 1.4. Historical Change in the Biogeochemical Cycling of Elements
Chapt. 2. Biological Necessity for and the Behaviors of Inorganic Elements 2.1. Introduction 2.2..Inorganic Elements in Biological Systems 2.2.1. Inorganic elements involved at molecular level 2.2.2. Inorganic elements involved at cellular level 2.2.3. Inorganic elements involved at physiological level 2.2.4. Biological systems involved in the metabolism of inorganic elements 2.3. Why have Organisms Chosen Specific Elements for their Specific Needs Basic Rules 2.4. Behaviors of Inorganic Elements-1-Fundamentals of Coordination Chemistry 2.4.1. Coordination compounds or metal complexes 2.4.2. Ligand field theory-how the predominant structure is determined 2.4.3. Thermodynamic tendency to form coordination compounds 2.4.4. Chelate effects 2.4.5. Ligand substitution reactions 2.4.6. Oxidation-reduction and reduction potential 2.4.7. Kinetic factors including long-range electron transference 2.5. Behaviors of Inorganic Elements-2-Organometallic Chemistry 2.5.1. Metal carbonyls and 18 electron rule 2.5.2. Other organometallic compounds 2.5.3. Some special types of reactions involving organometallic compounds
Chapt. 3. How Do Enzymes Work? 3.1. Enzymatic Enhancement of Reaction Rate – General Considerations 3.1.1. “Transition state” theory 3.1.2. The “Dynamic” effects 3.1.3. A Composite theory 3.2. Metalloenzymes and Metal-Activated Enzymes/Proteins
Chapt. 4. Reactions of Acid-Base Type and Functions of Metal Cations 4.1. General Considerations 4.1.1. Different types (definitions) of acid-base 4.1.2. Enzymes catalyzing reactions of acid-base type 4.1.3. Acidity scale and acid character of metal cations – prominence of Zn(II) and Mg(II) 4.1.4. Kinetic factors 4.1.5. The enhancement of reaction by amino acid residues in protein 4.2. Mg(II)-dependent Enzymes 4.2.1. Rubisco (Ribulose1,5-bisphosphate carboxylase/oxygenase) 4.2.1. Pyruvate kinase 4.3. Zn(II)-dependent Enzymes 4.3.1. Carbonic anhydrase 4.3.2. Thermolysin, carboxypeptidase A and others 4.3.3. Leucine amonopeptidase 4.3.4. Alkaline phosphatase and purple-acid phosphatase 4.3.5. Alcohol dehydrogenase 4.4. Other Cation-dependent Enzymes 4.4.1. Aconitase, an iron-sulfur enzyme, and others 4.4.2. Arginase – a Mn enzyme 4.4.3. Urease and other Ni-enzymes 4.5. Structural Effects of Metal Ions 4.6. Metal Ions and Polynucleic Acids (DNA and RNA) 4.6.1. General characteristics of interactions of metal ions with polynucleotides 18.104.22.168. Effects on structures 22.214.171.124. Catalytic metal ions in DNA polymerases and nucleases 4.6.2. Gene regulation and metal ions 4.6.2. Ribozymes
Chapt. 5. Reactions of Oxidation-Reduction Type including Electron Transfer Processes 5.1. General Consideration 5.1.1. Reduction potential 126.96.36.199. Heme proteins and enzymes 188.8.131.52. Iron-sulfur proteins 184.108.40.206. Copper proteins 220.127.116.11. Molybdenum proteins/tungsten proteins 5.1.2. Kinetic factors – electron transfer between and in protein(s) 5.2. Iron Enzymes and Proteins 5.2.1. Cytochromes and iron-sulfur electron transfer proteins 5.2.2. Nitrate reductase and nitric oxide reductase 5.2.3. Horse radish peroxidase (HRP), catalase and cytochrome c peroxidase 5.2.4. Hydrogenase 5.3. Copper Enzymes and Proteins 5.3.1. Blue copper proteins 5.3.2. Blue oxidases 5.3.3. Cytochrome c oxidase 5.3.4. Nitrite reductase and nitrous oxide reductase 5.3.5. Amine oxidases 5.3.6. Superoxide dismutase 5.4. Molybdenum Enzymes and Tungsten Enzymes 5.4.1. Xanthine oxidase and aldehyde oxidase 5.4.2. Sulfite oxidase and nitrate reductase (assimilatory) 5.4.3. DMSO reductase and nitrate reductase (respiratory) 5.4.4. Tungsten enzymes 5.5. Manganese Oxidoreductases 5.5.1. Manganese catalase 5.5.2. Water oxidase 5.6. Ni-containing Redox Enzymes 5.6.1. Ni-Fe (Se) hydrogenase 5.6.2. Carbon monoxide dehydrogenase (CODH) 5.6.3. Acetyl CoA synthase (ACS) 5.6.4. Methyl-coenzyme M reductase
Chapt. 6. Oxygen-Carrying Processes and Oxygenation Reactions 6.1. Chemistry of Oxygen, Dioxygen and Related Entities 6.1.1. The electronic structures 6.1.2. Basic reactions of O and O2 6.1.3. Reactions of ground states of O and O2 6.1.4. Interactions of ground state O2 with compounds of transition metals 6.1.5. Reactions of oxygen derivatives 6.2. Reversible O2 Binding – Oxygen Carriers – 6.3. Monoosygenases 6.3.1. Monoyxgenases dependent on cytochrome P-450 6.3.2. Non-heme mononuclear iron monooxygenases 6.3.3. Non-heme dinuclear iron monooxygenase 6.3.4. Copper monooxygenases 6.4. Dioxygenases 6.5. Prostaglandin Endoperoxide Synthase
Chapt. 7. Metal-Involving Free Radical Reactions 7.1. A Survey of Biologically Relevant Free Radicals 7.2. Why Radcials 7.3. Reactivities of Free Radicals 7.4. B12-Coenzyme (Adenosylcobalamin) Dependent Enzyme 7.4.1. Mutases, diol dehydratase and ethanolamine ammonia lyase 7.4.2. Ribonucelotide reductase (cobalamin dependent) 7.5. S-Adenosyl Methionine (SAM) Dependent Enzymes 7.6. Iron-Dependent Ribonucleotide Reductases 7.7. Galactose Oxidase 7.8. Other Examples
Chapt. 8. Nitrogen Fixation 8.1. Nitrogen Metabolism 8.2. Chemistry of N2 Reduction 8.3. Mo-dependent Nitrogenases 8.4. Other Nitrogenases
Chapt. 9. Other Essential Elements
9.2. Biochemistry of Nitrogen Compounds
9.3. Biochemistry of Phosphorus
9.4. Biochemistry of Sulfur Compounds
9.4.1. Cellular processes
9.4.2. Marine biogeochemical cycling
9.5.1. Chemistry of selenium as compared to that of sulfur
9.5.2. Glutathione and selenium – glutathione peroxidase
9.5.3. Thioredoxin reductase
9.5.4. Other selenium containing proteins/enzymes
9.7.1. Chemistry of silicon
9.7.2. Frustules of diatoms
9.7.3. Spicules in sponge
9.7.4. Other biological functions of silicon
9.8. Vanadium 9.8.1. Vanadins 9.8.2. Amavadin 9.8.3. Haloperoxidases 9.9. Chromium 9.10. Halogens and the Like 9.10.1. Formation of volatile halocarbons in macroalgae 9.10.2. HOX formation in mammals and others 18.104.22.168. Formation of HOX by fungal chlorperoxidase 22.214.171.124. Formation of HOX and others by mammalian peroxidases
Chapt. 10. Metal-related Physiology
10.1. Metabolism of Metallic Elements 10.1.1. Iron metabolism (in human) 10.1.1.1 Ferric reductase 10.1.1.2. Divalent metal transporter (DMT1) 10.1.1.3. Ferroxidase 10.1.1.4. Transferrin (Tf) and transerrin receptor (TfR) 10.1.1.5. Ferritin 10.1.1.6. Ferroportin (Fpn)/hepcidin 10.1.1.7. Regulation of ferritin and transferrin 10.1.1.8. Iron metabolism in bacteria, fungi and plants 10.1.2. Copper metabolism 10.2.1.1. An outline of copper metabolism in mammals 10.2.1.2. Copper metabolism in bacteria and plants 10.1.3. Zinc metabolism 10.1.3.1. In mammals 10.1.3.2. in E. coli 10.1.4. A Mg(II) transporter 10.2. Physiological Processes Played by Metallic Elements 10.2.1. Na/K-ATPase and Ca-ATPase 10.2.1.1. Mechanism 10.2.1.2. Ion selectivity in metal ion transporters and channels – a general discussion 10.2.2. Ca(II) – second messenger, and other functions 10.2.2.1. Control of cytoplasmic Ca(II) concentration 10.2.2.2. Basic mechanisms of Ca(II)-physiology 10.2.2.3. Synaptotagmin – as an example of physiology mediated by Ca(II) 10.2.2.4. Why calcium(II)? 10.2.3. ZEN 10.2.4. Sensors for small molecules 10.2.4.1. Oxygen sensors 10.2.4.2. CO-sensors 10.2.4.3. NO-sensors 10.2.4.4. H2 sensors 10.2.4.5. Redox sensors 10.2.5. Plant hormone, ethylene and copper 10.2.6. Magnetic navigation 10.2.7. Radiation shields 10.3. Biological Skeletons (Biominerals) 10.3.1. Calcium carbonate 10.3.2. Calcium oxalate 10.3.3. Calcium phosphate
Chapt. 11. Environmental Bioinorganic Chemistry 11.1. General Considerations 11.2. Toxicity of Inorganic Compounds 11.2.1. Abundance and toxicity 11.2.2. Toxicity of reactive oxygen species, and defense mechanisms 11.3. Molecular Mechanisms of Toxicity of Inorganic Compounds 11.3.1. Discrimination of elements by organisms – general considerations 11.3.2. Oxidative stress and metals and As – general effects 11.3.3. Individual element’s (acute) toxicity 126.96.36.199. Cd(II) and Hg(II) 188.8.131.52. Pb(II) 184.108.40.206. Organometallic compounds 220.127.116.11. Orgnotin compounds 18.104.22.168. Be(II), Al(III) 22.214.171.124. Tl(I) 126.96.36.199. Cr 188.8.131.52. Ni(II) 184.108.40.206. ANIONS 11.3.4. Alzheimer’s disease and metals 11.4. Biological Defenses against Toxicity 11.4.1. Biological defense against mercury 11.4.2. Metallothioneins and phytochelatins 220.127.116.11. Metallothioneins 18.104.22.168. Copper-thionein 22.214.171.124. Phytochelatins 126.96.36.199. Use of sulfide 11.4.3. Defense against lead 11.4.4. Biotransformation of arsenic 11.5. Bioremediaion of Metals 11.5.1. Biosorption by brown algae and by microbial surfactants 11.5.2. Phytoremediation (phytoextraction of metals from soil) 11.5.3. Phytoextraction by microalgae (remediation of polluted water) 11.5.4. Other types of bioremediation
Chapt. 12 Medical Applications of Inorganic Compounds: Medicinal Inorganic Chemistry 12.1. Introduction 12.2. Cancer Therapy 12.2.1. Platinum compounds 12.2.2. Bleomycin 12.2.3. Radioactive pharmaceuticals 12.3. Gold Compounds for Rheumatoid Arthritis 12.4. Vanadium Compounds for Diabetes 12.5. Lithium Compounds for Psychiatric Disorders 12.6. Other Potential Drugs Containing Inorganic Compounds 12.7. Daignostic (Imaging) Agents 12.7.1. Gd(III)-containing agents for MRI 12.7.2. 99mTc-radioactive diagnostic pharmaceuticals
- No. of pages:
- © Academic Press 2008
- 3rd July 2008
- Academic Press
- Paperback ISBN:
- eBook ISBN:
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