Biochemistry of Nonheme Iron

ISBN-13: 9781468437812 / Angielski / Miękka / 2012 / 436 str.

Anatoly Bezkorovainy

Opis

These two volumes will treat the two main structural categories of iron: heme and nonheme iron. In this volume on nonheme iron, the first in the series, Anatoly Bezkorovainy provides what we believe is the most comprehensive treatment of this important topic.

Spis treści

1. Tissue Iron and an Overview on Nonheme Iron Biochemistry.- 1.1 Introduction to Iron Metabolism.- 1.2 Historical Sketch of Iron Biology.- 1.3 Some Quantitative Data on Iron Distribution in Various Life Forms.- 1.4 Iron Determination in Biological Systems.- Summary.- References.- 2. Ferrokinetics.- 2.1 Classical Approach to Ferrokinetics.- 2.2 Compartment Models.- 2.3 Approaches to Ferrokinetics Based on the Probability Theory.- Summary.- List of Additional Abbreviations Used in Chapter 2.- References.- 3. Absorption of Nonheme Iron.- 3.1 Introduction.- 3.1.1 Quantitative Significance of Iron in the Body.- 3.1.2 Heme Iron.- 3.1.3 Nonheme Iron.- 3.2 Techniques of Measuring Absorption.- 3.2.1 Methods Using Stable Iron.- 3.2.2 Methods Using Radioiron.- 3.2.3 In Vitro Measurements.- 3.2.4 Administration of Dose.- 3.3 Mechanism of Iron Absorption.- 3.3.1 Role of the Stomach.- 3.3.2 Role of Bile.- 3.3.3 Role of the Pancreas.- 3.3.4 Role of the Intestine.- 3.4 Corporal Factors Affecting Iron Absorption.- 3.4.1 Physiological States.- 3.4.2 Iron Absorption during Disease.- 3.5 Intraluminal Factors Affecting Iron Absorption.- 3.5.1 Macronutrients.- 3.5.2 Micronutrients.- 3.5.3 Complexing Agents.- 3.5.4 Fortification Iron.- 3.6 Mucosal Factors Affecting Iron Absorption.- 3.7 Regulation of Iron Absorption.- 3.8 Groups at Risk.- 3.9 Fortification.- Summary.- References.- 4. Chemistry and Metabolism of the Transferrins.- 4.1 Introduction.- 4.2 The Levels of Transferrins in Biological Fluids.- 4.3 Isolation of the Transferrins.- 4.4 Physical Properties of the Transferrins.- 4.4.1 Hydrodynamic Parameters, Molecular Weights, and X-Ray Diffraction.- 4.4.2 Denaturation of the Transferrins.- 4.4.3 Quaternary Structure of the Transferrins.- 4.4.4 Secondary Structure of the Transferrins.- 4.5 Metal-Binding Properties of the Transferrins.- 4.5.1 Metal Ions that Are Bound by the Transferrins.- 4.5.2 The Binding of “Synergistic” Anions by the Transferrins.- 4.5.3 The Reaction of Iron with the Transferrins.- 4.5.4 Are the Two Iron-Binding Sites of the Transferrins Identical?.- 4.6 Distribution of Iron in Human Serum Transferrin in Vivo.- 4.7 Some Gross Differences between Iron-Free and Iron-Saturated Transferrins.- 4.8 The Iron-Binding Ligands of the Transferrins.- 4.9 Primary Structure of the Transferrins.- 4.9.1 Structure and Significance of the Carbohydrate Moiety of the Transferrins.- 4.9.2 Cyanogen Bromide Fragmentation of the Transferrins.- 4.9.3 Amino Acid Sequences of Cyanogen Bromide Fragments of Human Serotransferrin.- 4.9.4 Fragments of the Transferrins Containing a Single Iron-Binding Site.- 4.10 Microheterogeneity of the Transferrins.- 4.11 Metabolism of the Transferrins.- Summary.- References.- 5. Chemistry and Biology of Iron Storage.- 5.1 Distribution of Ferritin and Hemosiderin.- 5.2 Isolation of Ferritin.- 5.3 Physical-Chemical Properties of the Ferritins.- 5.3.1 Gross Structure of Ferritin.- 5.3.2 Molecular Weight of Ferritin and Apoferritin.- 5.3.3 Subunits of the Ferritins.- 5.3.4 Distribution of Iron among Ferritin Oligomers and Isoferritins.- 5.3.5 Composition and Primary Structure of the Ferritins.- 5.3.6 Secondary and Tertiary Structure of Ferritin Subunits.- 5.4 Metabolism of Ferritin.- 5.5 Iron Uptake and Release by Ferritin and Apoferritin.- 5.6 Ferritin and Tissue Iron Metabolism.- 5.6.1 Iron Metabolism in the Liver.- 5.6.2 Iron Metabolism in the Reticuloendothelial System.- 5.6.3 Iron Overload.- 5.6.4 Serum Ferritin.- 5.6.5 Intestinal Mucosal Cells and Iron Metabolism.- Summary.- References.- 6. The Interaction of Nonheme Iron with Immature Red Cells.- 6.1 Introduction.- 6.2 Early Investigations on Serotransferrin-Immature Red Cell Interactions.- 6.3 The Mechanism of Serotransferrin-Immature Red Cell Interaction.- 6.4 Molecular Properties of Serotransferrin and its Effect on the Interaction with Immature Red Cells.- 6.5 Transferrin Receptors in the Immature Red Cells.- 6.6 Iron Removal from Serotransferrin.- Summary.- References.- 7. Microbial Iron Uptake and the Antimicrobial Properties of the Transferrins.- 7.1 Introduction.- 7.2 Structure of Siderophores.- 7.2.1 Catechol-like Siderophores.- 7.2.2 Hydroxamate-like Siderophores.- 7.3 Chemical and Physical Properties of the Siderophores.- 7.4 Metabolism and Biological Properties of the Siderophores.- 7.4.1 Biosynthesis of Siderophores.- 7.4.2 Mode of Iron Delivery to Microbial Cells by Siderophores.- 7.4.3 Energy Requirements during Iron Uptake by Microorganisms.- 7.4.4 Control of Siderophore Biosynthesis.- 7.5 Siderophores of Mammalian Origin.- 7.6 Iron Chelators in Clinical Practice.- 7.7 Antimicrobial Properties of the Transferrins.- 7.7.1 In Vitro Effects of Transferrins on Microbial Growth.- 7.7.2 Iron Status and Infection in Whole Organisms.- 7.7.3 Lactoferrin and Protection of the Breast-Fed Infant against Digestive and Systemic Disease.- Summary.- References.- 8. The Iron-Sulfur Proteins.- 8.1 Introduction and Classification.- 8.2 Rubredoxins.- 8.3 Ferredoxins.- 8.3.1 Plant-Type Ferredoxins (Two-Iron Clusters).- 8.3.2 Bacterial-Type Ferredoxins Containing Two Four-Iron Clusters.- 8.3.3 Bacterial Ferredoxins with One Four-Iron Cluster.- 8.3.4 Removal of Iron Clusters from Ferredoxins.- 8.3.5 Functions of Bacterial Ferredoxins.- 8.3.6 Evolution of Ferredoxins.- 8.4 Iron-Sulfur Proteins and Nitrogen Fixation.- 8.5 Iron-Sulfur Proteins of Mammalian Electron Transport Mechanisms.- 8.5.1 Adrenodoxin and the Biosynthesis of Steroid Hormones.- 8.5.2 Hydroxylation of 25-Hydroxycholecalciferol.- 8.5.3 Iron-Sulfur Centers in the Oxidative Phosphorylation Pathway.- 8.6 Miscellaneous Iron-Sulfur Proteins.- Summary.- References.- 9. Miscellaneous Aspects of Iron Metabolism.- 9.1 Introduction.- 9.2 Phosvitin, an Egg Iron-Binding Phosphoprotein.- 9.3 The Oxygenases.- 9.3.1 Phenylalanine Hydroxylase.- 9.3.2 Tyrosine and Tryptophan Hydroxylases.- 9.3.3 Pyrocatechase (Catechol-1, 2-dioxygenase).- 9.3.4 Protocatechuate-3, 4-dioxygenase.- 9.3.5 4-Hydroxyphenylpyruvate Dioxygenase.- 9.3.6 Proline Hydroxylase.- 9.4 Hemerythrins.- 9.5 Iron Bacteria.- 9.6 Metalloserotransferrin as a Lymphocyte Growth Promoter.- Summary.- References.- Suggested Reading.