Sykes / Mauk Heme-Fe Proteins

1. Auflage 2000
ISBN: 978-0-08-052449-8
Verlag: Elsevier Science & Techn.
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, 400 Seiten, Web PDF

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.

Autoren/Hrsg.

Sykes, AG

Mauk, Grant

Inhaltsverzeichnis

1;Cover;1
2;Copyright Page ;5
3;Contents;6
4;Chapter 1. Clinical Reactivity of the Active Site of Myoglobin;10
4.1;I. Introduction;10
4.2;II. Cloning and Expression of Recombinant Myoglobin;12
4.3;III. Active Site Variants of Myoglobin;13
4.4;IV. Electron Transfer Reactions of Myoglobin;17
4.5;V. Peroxidase Activity;29
4.6;VI. Lipoxygenase Activity;38
4.7;VII. Monooxygenase Activity;39
4.8;VIII. Coupled Oxidation;42
4.9;IX. Sulfmyoglobin;46
4.10;X. Other Reactions of Myoglobin;47
4.11;XI. Concluding Remarks;48
4.12;References;49
5;Chapter 2. Enzymology and Structure of Catalases;60
5.1;I. Introduction;61
5.2;II. Categorization;62
5.3;III. Physiology;65
5.4;IV. Kinetics;68
5.5;V. Structure of Type A Catalases;81
5.6;VI. Structure of Type B Catalase-Peroxidases;104
5.7;VII. Structure of Chloroperoxidase;106
5.8;VIII. Mechanism of the Catalytic Reaction;106
5.9;IX. Summary;111
5.10;References;112
6;Chapter 3. Horseradish Peroxidase;116
6.1;I. Introduction;117
6.2;II. Biochemistry and Molecular Biology;118
6.3;III. General Features of the Enzyme;125
6.4;IV. Structure and Function;133
6.5;V. Applications;155
6.6;References;161
7;Chapter 4. Structure and Enzymology of Diheme Enzymes: Cytochrome cd1 Nitrate and Cytochrome c Peroxidase;172
7.1;I. Introduction;172
7.2;II. Cytochromes cd1;176
7.3;III. Diheme Cytochrome c Peroxidases;194
7.4;References;210
8;Chapter 5. Binding and Transport of Iron-Porphyrins by Hemopexin;214
8.1;I. Introduction;214
8.2;II. Biological Properties of Hemopexin;216
8.3;III. Biological Activities of Hemopexin;217
8.4;IV. Physical–Chemical Properties of Hemopexin;221
8.5;V. Hemopexin Receptor Properties on Heme–Hemopexin;239
8.6;VI. Conclusion;244
8.7;References;245
9;Chapter 6. Structures of Gas-Generating Heme Enzymes Nitric Oxide Synthase and Heme Oxygenase;252
9.1;I. Introduction;253
9.2;II. Biological Targets of NO and CO Action;254
9.3;III. Overview of Oxygen Activating Heme Enzymes;255
9.4;IV. Background on NOS;258
9.5;V. NOS Structure;260
9.6;VI. NOS Catalytic Structure;275
9.7;VII. Background on HO;281
9.8;VIII. HO Structure;282
9.9;IX. HO Catalytic Mechanism;289
9.10;X. Outlook;295
9.11;References;296
10;Chapter 7. The Nitric Oxide-Releasing Heme Proteins From the Saliva of the Blood-Sucking Insect Rhodnius prolixus;304
10.1;I. Introduction;305
10.2;II. Spectroscopic Characterization of the Nitrophorins;314
10.3;III. Crystallization and Structural Determination of Nitrophorins;334
10.4;IV. Kinetics and Thermodynamics of Ligand Binding;346
10.5;V. Reduction Potentials of Nitrophorins in the Absence and Presence of No, Histamine, and Other Ligands;352
10.6;VI. Summary and Future Directions;360
10.7;References;362
11;Chapter 8. Heme Oxygenase Structure and Mechanism;368
11.1;I. Introduction;368
11.2;II. Biological Function of Heme Oxygenase;372
11.3;III. Heme Oxygenase Model Systems;373
11.4;IV. Heme Oxygenase The Protein;376
11.5;V. Human HO-1 Crystal Structure;383
11.6;VI. Interaction with Cytochrome P450 Reductase;385
11.7;VII. Gaseous Ligands;386
11.8;VIII. Substrate Specificity;388
11.9;IX. The First Stage: a-meso-Hydroxylation;390
11.10;X. The Second Stage: a-meso-Hydroxyheme to Verdoheme;397
11.11;XI. The Third Stage: Verdoheme to Biliverdin;401
11.12;XII. Kinetics of the Heme Oxygenase Reaction Sequence;403
11.13;XIII. Implications of Electrophilic Heme Oxidation by an FeIII–OOH Intermediate;405
11.14;XIV. Heme Degradation in Plants and Bacteria;407
11.15;References;411
12;Chapter 9. De Novo Design and Synthesis of Heme Proteins;418
12.1;I. Introduction;418
12.2;II. Natural Protein Engineering;420
12.3;III. De Novo Heme Proteins;426
12.4;IV. Physical/Electrochemical Studies of de Novo Designed Heme Proteins;442
12.5;V. Functional Aspects;447
12.6;References;458
13;Index;466
14;Contents of Previous Volumes;478