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Bioinorganic Chemistry - 1st Edition - ISBN: 9780120887569, 9780080886978

Bioinorganic Chemistry

1st Edition

A Survey

Author: Ei-Ichiro Ochiai
Paperback ISBN: 9780120887569
eBook ISBN: 9780080886978
Imprint: Academic Press
Published Date: 3rd July 2008
Page Count: 360
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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.

Key Features

  • 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 *

Table of Contents

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 Monosasccharides Polysaccharides and derivatives
0.3.2. Lipids Fats and phospholipids Steroids
0.3.3. Proteins and amino acids Structures Reactions – formation and hydrolysis of protein
0.3.4. Nucleotides, vitamins (coenzymes) and others Coenzymes Nucleotides Other vitamins Hormone, neurotransmitters and others
0.3.5. DNA/RNA (Polynucleotide) Structures Reactions
0.4. Types of Biochemical Reactions
0.4.1. Reactions of acid-base type
0.4.2. Reactions of oxidation-reduction type The idea of oxidation state The oxidation state of “C” in organic compounds and recognition of oxidation-reduction reactions 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 Effects on structures 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 Heme proteins and enzymes Iron-sulfur proteins Copper proteins 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
9.1. Introduction
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. Selenium
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
9.6. Boron
9.7. Silicon
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 Formation of HOX by fungal chlorperoxidase 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) Ferric reductase Divalent metal transporter (DMT1) Ferroxidase Transferrin (Tf) and transerrin receptor (TfR) Ferritin Ferroportin (Fpn)/hepcidin Regulation of ferritin and transferrin Iron metabolism in bacteria, fungi and plants
10.1.2. Copper metabolism An outline of copper metabolism in mammals Copper metabolism in bacteria and plants
10.1.3. Zinc metabolism In mammals 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 Mechanism Ion selectivity in metal ion transporters and channels – a general discussion
10.2.2. Ca(II) – second messenger, and other functions Control of cytoplasmic Ca(II) concentration Basic mechanisms of Ca(II)-physiology Synaptotagmin – as an example of physiology mediated by Ca(II) Why calcium(II)?
10.2.3. ZEN
10.2.4. Sensors for small molecules Oxygen sensors CO-sensors NO-sensors H2 sensors 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 Cd(II) and Hg(II) Pb(II) Organometallic compounds Orgnotin compounds Be(II), Al(III) Tl(I) Cr Ni(II) 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 Metallothioneins Copper-thionein Phytochelatins 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


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© Academic Press 2008
3rd July 2008
Academic Press
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Ei-Ichiro Ochiai

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