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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...

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Sykes, A. G.
Formato: Electrónico eBook
Idioma:Inglés
Publicado: San Diego : Academic Press, �2001.
Colección:Advances in inorganic chemistry ; v. 51.
Temas:
Acceso en línea:Texto completo

MARC

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245 0 0 |a Heme-Fe proteins /  |c edited by A.G. Sykes. 
260 |a San Diego :  |b Academic Press,  |c �2001. 
300 |a 1 online resource (viii, 472 pages). 
336 |a text  |b txt  |2 rdacontent 
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490 1 |a Advances in inorganic chemistry ;  |v v. 51 
504 |a Includes bibliographical references and index. 
588 0 |a Print version record. 
520 |a 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. 
505 0 |a 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 
505 8 |a 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 
505 8 |a 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 
505 8 |a 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 
505 8 |a 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 
650 0 |a Hemoproteins. 
650 0 |a Bioinorganic chemistry. 
650 6 |a H�emoprot�eines.  |0 (CaQQLa)201-0041818 
650 6 |a Chimie bio-inorganique.  |0 (CaQQLa)201-0237294 
650 7 |a hemoprotein.  |2 aat  |0 (CStmoGRI)aat300192942 
650 7 |a Bioinorganic chemistry  |2 fast  |0 (OCoLC)fst00832183 
650 7 |a Hemoproteins  |2 fast  |0 (OCoLC)fst00955100 
700 1 |a Sykes, A. G. 
830 0 |a Advances in inorganic chemistry ;  |v v. 51. 
856 4 0 |u https://sciencedirect.uam.elogim.com/science/book/9780120236510  |z Texto completo