Heme-Fe Proteins (eBook)

Cover 1
Copyright Page 5
Contents 6
Chapter 1. Clinical Reactivity of the Active Site of Myoglobin 10
I. Introduction 10
II. Cloning and Expression of Recombinant Myoglobin 12
III. Active Site Variants of Myoglobin 13
IV. Electron Transfer Reactions of Myoglobin 17
V. Peroxidase Activity 29
VI. Lipoxygenase Activity 38
VII. Monooxygenase Activity 39
VIII. Coupled Oxidation 42
IX. Sulfmyoglobin 46
X. Other Reactions of Myoglobin 47
XI. Concluding Remarks 48
References 49
Chapter 2. Enzymology and Structure of Catalases 60
I. Introduction 61
II. Categorization 62
III. Physiology 65
IV. Kinetics 68
V. Structure of Type A Catalases 81
VI. Structure of Type B Catalase-Peroxidases 104
VII. Structure of Chloroperoxidase 106
VIII. Mechanism of the Catalytic Reaction 106
IX. Summary 111
References 112
Chapter 3. Horseradish Peroxidase 116
I. Introduction 117
II. Biochemistry and Molecular Biology 118
III. General Features of the Enzyme 125
IV. Structure and Function 133
V. Applications 155
References 161
Chapter 4. Structure and Enzymology of Diheme Enzymes: Cytochrome cd1 Nitrate and Cytochrome c Peroxidase 172
I. Introduction 172
II. Cytochromes cd1 176
III. Diheme Cytochrome c Peroxidases 194
References 210
Chapter 5. Binding and Transport of Iron-Porphyrins by Hemopexin 214
I. Introduction 214
II. Biological Properties of Hemopexin 216
III. Biological Activities of Hemopexin 217
IV. Physical–Chemical Properties of Hemopexin 221
V. Hemopexin Receptor Properties on Heme–Hemopexin 239
VI. Conclusion 244
References 245
Chapter 6. Structures of Gas-Generating Heme Enzymes Nitric Oxide Synthase and Heme Oxygenase 252
I. Introduction 253
II. Biological Targets of NO and CO Action 254
III. Overview of Oxygen Activating Heme Enzymes 255
IV. Background on NOS 258
V. NOS Structure 260
VI. NOS Catalytic Structure 275
VII. Background on HO 281
VIII. HO Structure 282
IX. HO Catalytic Mechanism 289
X. Outlook 295
References 296
Chapter 7. The Nitric Oxide-Releasing Heme Proteins From the Saliva of the Blood-Sucking Insect Rhodnius prolixus 304
I. Introduction 305
II. Spectroscopic Characterization of the Nitrophorins 314
III. Crystallization and Structural Determination of Nitrophorins 334
IV. Kinetics and Thermodynamics of Ligand Binding 346
V. Reduction Potentials of Nitrophorins in the Absence and Presence of No, Histamine, and Other Ligands 352
VI. Summary and Future Directions 360
References 362
Chapter 8. Heme Oxygenase Structure and Mechanism 368
I. Introduction 368
II. Biological Function of Heme Oxygenase 372
III. Heme Oxygenase Model Systems 373
IV. Heme Oxygenase The Protein 376
V. Human HO-1 Crystal Structure 383
VI. Interaction with Cytochrome P450 Reductase 385
VII. Gaseous Ligands 386
VIII. Substrate Specificity 388
IX. The First Stage: a-meso-Hydroxylation 390
X. The Second Stage: a-meso-Hydroxyheme to Verdoheme 397
XI. The Third Stage: Verdoheme to Biliverdin 401
XII. Kinetics of the Heme Oxygenase Reaction Sequence 403
XIII. Implications of Electrophilic Heme Oxidation by an FeIII–OOH Intermediate 405
XIV. Heme Degradation in Plants and Bacteria 407
References 411
Chapter 9. De Novo Design and Synthesis of Heme Proteins 418
I. Introduction 418
II. Natural Protein Engineering 420
III. De Novo Heme Proteins 426
IV. Physical/Electrochemical Studies of de Novo Designed Heme Proteins 442
V. Functional Aspects 447
References 458
Index 466
Contents of Previous Volumes 478