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Heme-Fe proteins /
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 referenc...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
San Diego :
Academic Press,
�2001.
|
| Colección: | Advances in inorganic chemistry ;
v. 51. |
| Temas: | |
| Acceso en línea: | Texto completo |
Tabla de Contenidos:
- Front Cover; Advances in Inorganic Chemistry; Copyright Page; Contents; Chapter 1. Clinical Reactivity of the Active Site of Myoglobin; I. Introduction; II. Cloning and Expression of Recombinant Myoglobin; III. Active Site Variants of Myoglobin; IV. Electron Transfer Reactions of Myoglobin; V. Peroxidase Activity; VI. Lipoxygenase Activity; VII. Monooxygenase Activity; VIII. Coupled Oxidation; IX. Sulfmyoglobin; X. Other Reactions of Myoglobin; XI. Concluding Remarks; References; Chapter 2. Enzymology and Structure of Catalases; I. Introduction; II. Categorization; III. Physiology
- IV. KineticsV. Structure of Type A Catalases; VI. Structure of Type B Catalase-Peroxidases; VII. Structure of Chloroperoxidase; VIII. Mechanism of the Catalytic Reaction; IX. Summary; References; Chapter 3. Horseradish Peroxidase; I. Introduction; II. Biochemistry and Molecular Biology; III. General Features of the Enzyme; IV. Structure and Function; V. Applications; References; Chapter 4. Structure and Enzymology of Diheme Enzymes: Cytochrome cd1 Nitrate and Cytochrome c Peroxidase; I. Introduction; II. Cytochromes cd1; III. Diheme Cytochrome c Peroxidases; References
- Chapter 5. Binding and Transport of Iron-Porphyrins by HemopexinI. Introduction; II. Biological Properties of Hemopexin; III. Biological Activities of Hemopexin; IV. Physical-Chemical Properties of Hemopexin; V. Hemopexin Receptor Properties on Heme-Hemopexin; VI. Conclusion; References; Chapter 6. Structures of Gas-Generating Heme Enzymes Nitric Oxide Synthase and Heme Oxygenase; I. Introduction; II. Biological Targets of NO and CO Action; III. Overview of Oxygen Activating Heme Enzymes; IV. Background on NOS; V. NOS Structure; VI. NOS Catalytic Structure; VII. Background on HO
- VIII. HO StructureIX. HO Catalytic Mechanism; X. Outlook; References; Chapter 7. The Nitric Oxide-Releasing Heme Proteins From the Saliva of the Blood-Sucking Insect Rhodnius prolixus; I. Introduction; II. Spectroscopic Characterization of the Nitrophorins; III. Crystallization and Structural Determination of Nitrophorins; IV. Kinetics and Thermodynamics of Ligand Binding; V. Reduction Potentials of Nitrophorins in the Absence and Presence of No, Histamine, and Other Ligands; VI. Summary and Future Directions; References; Chapter 8. Heme Oxygenase Structure and Mechanism; I. Introduction
- II. Biological Function of Heme OxygenaseIII. Heme Oxygenase Model Systems; IV. Heme Oxygenase The Protein; V. Human HO-1 Crystal Structure; VI. Interaction with Cytochrome P450 Reductase; VII. Gaseous Ligands; VIII. Substrate Specificity; IX. The First Stage a-meso-Hydroxylation; X. The Second Stage a-meso-Hydroxyheme to Verdoheme; XI. The Third Stage Verdoheme to Biliverdin; XII. Kinetics of the Heme Oxygenase Reaction Sequence; XIII. Implications of Electrophilic Heme Oxidation by an FeIII-OOH Intermediate; XIV. Heme Degradation in Plants and Bacteria; References