Heme-Fe Proteins
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Table of contents
- Copyright Pageiv
- Contentsv
- Chapter 1. Clinical Reactivity of the Active Site of Myoglobin1
- I. Introduction1
- II. Cloning and Expression of Recombinant Myoglobin3
- III. Active Site Variants of Myoglobin4
- IV. Electron Transfer Reactions of Myoglobin8
- V. Peroxidase Activity20
- VI. Lipoxygenase Activity29
- VII. Monooxygenase Activity30
- VIII. Coupled Oxidation33
- IX. Sulfmyoglobin37
- X. Other Reactions of Myoglobin38
- XI. Concluding Remarks39
- References40
- Chapter 2. Enzymology and Structure of Catalases51
- I. Introduction52
- II. Categorization53
- III. Physiology56
- IV. Kinetics59
- V. Structure of Type A Catalases72
- VI. Structure of Type B Catalase-Peroxidases95
- VII. Structure of Chloroperoxidase97
- VIII. Mechanism of the Catalytic Reaction97
- IX. Summary102
- References103
- Chapter 3. Horseradish Peroxidase107
- I. Introduction108
- II. Biochemistry and Molecular Biology109
- III. General Features of the Enzyme116
- IV. Structure and Function124
- V. Applications146
- References152
- Chapter 4. Structure and Enzymology of Diheme Enzymes: Cytochrome cd1 Nitrate and Cytochrome c Perox163
- I. Introduction163
- II. Cytochromes cd1167
- III. Diheme Cytochrome c Peroxidases185
- References201
- Chapter 5. Binding and Transport of Iron-Porphyrins by Hemopexin205
- I. Introduction205
- II. Biological Properties of Hemopexin207
- III. Biological Activities of Hemopexin208
- IV. Physical–Chemical Properties of Hemopexin212
- V. Hemopexin Receptor Properties on Heme–Hemopexin230
- VI. Conclusion235
- References236
- Chapter 6. Structures of Gas-Generating Heme Enzymes Nitric Oxide Synthase and Heme Oxygenase243
- I. Introduction244
- II. Biological Targets of NO and CO Action245
- III. Overview of Oxygen Activating Heme Enzymes246
- IV. Background on NOS249
- V. NOS Structure251
- VI. NOS Catalytic Structure266
- VII. Background on HO272
- VIII. HO Structure273
- IX. HO Catalytic Mechanism280
- X. Outlook286
- References287
- Chapter 7. The Nitric Oxide-Releasing Heme Proteins From the Saliva of the Blood-Sucking Insect Rhod295
- I. Introduction296
- II. Spectroscopic Characterization of the Nitrophorins305
- III. Crystallization and Structural Determination of Nitrophorins325
- IV. Kinetics and Thermodynamics of Ligand Binding337
- V. Reduction Potentials of Nitrophorins in the Absence and Presence of No, Histamine, and Other Liga343
- VI. Summary and Future Directions351
- References353
- Chapter 8. Heme Oxygenase Structure and Mechanism359
- I. Introduction359
- II. Biological Function of Heme Oxygenase363
- III. Heme Oxygenase Model Systems364
- IV. Heme Oxygenase The Protein367
- V. Human HO-1 Crystal Structure374
- VI. Interaction with Cytochrome P450 Reductase376
- VII. Gaseous Ligands377
- VIII. Substrate Specificity379
- IX. The First Stage: a-meso-Hydroxylation381
- X. The Second Stage: a-meso-Hydroxyheme to Verdoheme388
- XI. The Third Stage: Verdoheme to Biliverdin392
- XII. Kinetics of the Heme Oxygenase Reaction Sequence394
- XIII. Implications of Electrophilic Heme Oxidation by an FeIII–OOH Intermediate396
- XIV. Heme Degradation in Plants and Bacteria398
- References402
- Chapter 9. De Novo Design and Synthesis of Heme Proteins409
- I. Introduction409
- II. Natural Protein Engineering411
- III. De Novo Heme Proteins417
- IV. Physical/Electrochemical Studies of de Novo Designed Heme Proteins433
- V. Functional Aspects438
- References449
- Index457
- Contents of Previous Volumes469
Advances in Inorganic Chemistry presents timely and informative summaries of the current progress in a variety of subject areas within inorganic chemistry, ranging from bioinorganic to solid state. This acclaimed serial features reviews written by experts in the area and is an indispensable reference to advanced researchers. Each volume of Advances in Inorganic Chemistry contains an index, and each chapter is fully referenced.