Note: Front Cover -- Oxidases and Related Redox Systems -- Copyright Page -- Table of Contents -- PREFACE -- PART I: ELECTRON TRANSFER RELATED TO OXYGEN BIOCHEMISTRY -- Chapter 1. On Quantum, Classical and Semiclassical Calculations of Electron Transfer Rates -- ABSTRACT -- INTRODUCTION -- CLASSICAL EXPRESSION FOR RATE CONSTAN -- QUANTUM ASPECTS OF THE NUCLEAR MOTION -- SUMMARY OF NUMERICAL RESULTS -- ACKNOWLEDGMENT -- DISCUSSION -- REFERENCES -- Chapter 2. Theory of Ultrafast Electron Transfer in Bacterial Photosynthesis -- I. INTRODUCTORY REMARKS -- II. IS CONVENTIONAL ET THEORY APPLICABLE? -- III. COMPETITION BETWEEN ET AND VR -- IV. EPILOGUE -- DISCUSSION -- REFERENCES -- Chapter 3. The Mechanism of Electron Transfer in the Electron Transport Chain -- DISCUSSION -- REFERENCES -- Chapter 4. Outer Sphere Electron Transfer Between Iron Porphyrins -- PRE-DISCUSSION -- ACKNOWLEDGEMENT -- POST-DISCUSSION -- REFERENCES AND NOTES -- Chapter 5. The Nature of the Primary Oxidants in Oxidations Mediated by Metal Ions -- SCHEME I -- SCHEME II -- DISCUSSION -- REFERENCES AND NOTES -- PART II: ACTIVE AND TOXIC STATES OF OXYGEN AND SUPEROXIDE -- Chapter 6. On the Question of Superoxide Toxicity and the Biological Function of Superoxide Dismutases -- INTRODUCTION -- FORMATION OF SUPEROXIDE IN BIOLOGICAL SYSTEMS -- SUMMARY OF CHEMICAL PROPERTIES OF AQUEOUS SUPEROXIDE -- SUPEROXIDE TOXICITY -- EXTRAPOLATION FROM IN VITRO TO IN VIVO CONDITIONS -- SUPEROXIDE DISMUTASE ACTIVITY AS A TRIVIAL REACTION? -- BIOLOGICAL DISTRIBUTION AND THE FUNCTION OF SUPEROXIDE DISMUTASES -- SUMMARY -- ACKNOWLEDGEMENTS -- DISCUSSION I -- DISCUSSION II -- DISCUSSION III -- NOTES TO TEXT -- REFERENCES FROM TEXT -- Chapter 7. Exacerbations of Oxygen Toxicity by Redox Active Compounds -- INTRODUCTION -- DISCUSSION -- REFERENCES. , Chapter 8. Se and Non-Se Glutathione Peroxidases: Enzymology and Cell Physiology -- INTRODUCTION -- Se GSH PEROXIDASE -- NON-Se GSH PEROXIDASE -- CELL PHYSIOLOGY -- SUMMARY -- REFERENCES -- PART III: COPPER CATALYZED REACTIONS OF MOLECULAR OXYGEN, MONONUCLEAR CU -- Chapter 9. Chemistry of Copper(III) -Peptide Complexes -- INTRODUCTION -- SUMMARY -- ACKNOWLEDGMENT -- DISCUSSION -- REFERENCES -- Chapter 10. Is Trivalent Copper a Viable Oxidation State in the Enzymatic Turnover of Copper Proteins? -- ABSTRACT -- THE FORMATION OF Cu (III) FROM LOWER OXIDATION STATES OF COPPER -- X-RAY ABSORPTION EDGE SPECTROSCOPY -- ABSORPTION EDGE STUDIES IN THE SOLID STATE -- ABSORPTION EDGE STUDIES IN SOLUTION -- X-RAY ABSORPTION EDGES OF GALACTOSE OXIDASE -- ABSORPTION EDGE STUDIES OF MODEL COMPOUNDS FOR GALACTOSE OXIDASE REACTED WITH FERRICYANIDE -- SUMMARY -- ACKNOWLEDGEMENT -- DISCUSSION -- REFERENCES -- Chapter 11. Studies on the Mechanism of Action of the Copper (II) Enzyme, Galactose Oxidase -- SUMMARY -- INTRODUCTION -- MATERIALS AND METHODS -- RESULTS AND DISCUSSION -- DISCUSSION -- REFERENCES -- PART IV: BINUCLEAR CU CLUSTERS IN OXYGEN METABOLISM -- Chapter 12. Comparison of the Active Sites of Molluscan and Arthropodan Hemocyanins -- I. FUNCTIONAL DOMAINS OF MOLLUSCAN HEMOCYANINS AND SUBUNITS OF ARTHROPODAN HEMOCYANINS -- II. CIRCULAR-DIHROIC SPECTRA OF OXYHEMOCYANINS -- III. THE BINDING OF THIOCYANATE TO MOLLUSCAN DEOXYHEMOCYANIN -- IV. FORMATION AND PROPERTIES OF METHEMOCYANINS -- V. THE REGENERATION OF METHEMOCYANINS -- VI. CONCLUDING REMARKS -- ACKNOWLEDGEMENTS -- DISCUSSION -- REFERENCES -- Chapter 13. Chemical and Spectroscopic Studies of the Binuclear Copper Active Site -- MET APO HEMOCYANIN -- HALF MET HEMOCYANIN -- DIMER HEMOCYANIN -- MET HEMOCYANIN -- ACKNOWLEDGEMENTS -- DISCUSSION -- REFERENCES. , Chapter 14. Hemocyanin Active Site Characterization by EXAFS and Resonance Raman Spectroscopy -- I. INTRODUCTION -- II. X-RAY ABSORPTION EDGE STRUCTURE -- III. EXAFS ANALYSIS -- IV. RESONANCE RAMAN SPECTRA -- V. A STRUCTURAL MODEL -- ACKNOWLEDGEMENTS -- DISCUSSION -- REFERENCES -- Chapter 15. Reaction Inactivation of Tyrosinase -- INTRODUCTION -- MATERIALS AND METHODS -- RESULTS AND DISCUSSION -- DISCUSSION -- REFERENCES -- PART V: FLAVIN CATALYZED REACTIONS OF MOLECULAR OXYGEN -- Chapter 16. DT Diaphorase: Properties, Reaction Mechanism, Metabolic Function. A Progress Report -- INTRODUCTION -- PURIFICATION AND PROPERTIES -- REACTION MECHANISM -- METABOLIC FUNCTION -- ACKNOWLEDGEMENTS -- DISCUSSION -- REFERENCES -- Chapter 17. Transformations of Flavin and Pteridine Intermediates in Oxygen Transfer Models -- I. INTRODUCTION -- II. TRANSIENT CARBONYL OXIDES AS SUGGESTED BY VARIOUS SPIROHYDANTOIN FORMATIONS -- III. TRANSFORMATIONS INVOLVING SECONDARY, NUCLEOPHILIC ADDITIONS -- IV. ESR-SILENT BLUE FLAVIN TRANSIENTS -- CONCLUSION -- DISCUSSION -- REFERENCES -- Chapter 18. The Role of the Apoprotein in Directing Pathways of Flavin Catalysis -- I. INTRODUCTION -- II. CHEMICAL AND BIOCHEMICAL ACTIVITIES OF THE FLAVIN-CHROMOPHORE -- III. QUESTIONS TOWARD A RATIONAL CLASSIFICATION -- IV. FUNCTIONAL CLASSIFICATION OF FLAVOPROTEINS -- V. STRUCTURAL CHARACTERISTICS OF FLAVOPROTEIN CLASSES (TABLE I) -- VI. THE MECHANISM OF FLAVIN-DEPENDENT OXYGEN-ACTIVATION -- VII. "N(5) VERSUS N(1)/O(2α)-BLOCKING" IN TERMS OF CHEMICAL STRUCTURE -- DISCUSSION -- REFERENCES -- Chapter 19. Lipid Environment of Monoamine Oxidase -- I. INTRODUCTION -- II. FRACTIONATION OF THE ENZYME BY AFFINITY CHROMATOGRAPHY -- III. DEPLETION OF LIPIDS FROM ENZYME PREPARATION -- IV. INCORPORATION OF LIPID-DEPLETED ENZYME INTO LIPOSOMES -- DISCUSSION -- REFERENCES -- Chapter 20. 4a-Peroxyflavins. , INTRODUCTION -- THE REACTION OF OXYGEN WITH N5-ALKYL 1,5-DIHYDROFLAVINS -- THE 4A-HYDROPEROXYFLAVIN MOIETY AS AN INTERMEDIATE IN THE REACTIONS OF EXTERNAL FLAVOPROTEIN MONOOXYGENASES -- OXYGEN INSERTION REACTIONS OF N5 -ETHYL-4A-HYDROPEROXYISOALLOXAZINES -- ACKNOWLEDGEMENTS -- DISCUSSION -- REFERENCES -- Chapter 21. Implications Concerning the Physiological Function of D-Amino Acid Oxidase as Derived from Inhibition Studies -- ACKNOWLEDGEMENT -- REFERENCES -- PART VI: IRON (NON-HEME) CATALYZED REACTIONS OF MOLECULAR OXYGEN -- Chapter 22. Resonance Raman Spectroscopic Studies of Non-heme-iron Dioxygenases -- I. INTRODUCTION -- II. RESONANCE RAMAN SPECTROSCOPY OF METALLOPROTEINS -- III. PROTOCATECHUATE 3,4-DIOXYGENASE AND PYROCATECHASE -- IV. RESONANCE RAMAN STUDIES OF DIOXYGENASES -- V. MECHANISTIC IMPLICATIONS: ESO2 = EP -- ACKNOWLEDGMENT -- DISCUSSION -- REFERENCES -- Chapter 23. Protocatechuate Dioxygenases: Structural and Mechanistic Studies -- I. INTRODUCTION -- II. DIOXYGENASE REACTIONS -- III. STRUCTURE OF PROTOCATECHUATE DIOXYGENASES -- IV. IRON SITE STRUCTURE -- V. MECHANISM -- ACKNOWLEDGEMENT -- REFERENCES -- Chapter 24. On the Mechanism of Lipoxygenase Catalysis -- INTRODUCTION -- SOYBEAN LIPOXYGENASE -- THE OXYGENATION REACTION -- ANAEROBIC REACTION -- AEROBIC REACTION -- ROLE OF IRON -- ACKNOWLEDGEMENTS -- DISCUSSION -- REFERENCES -- Chapter 25. Iron, an Essential Component of 4-Hydroxyphenylpyruvate Dioxygenase from Pseudomonas sp. Strain P.J. 874 -- INTRODUCTION -- MATERIALS AND METHODS -- RESULTS -- SUMMARY -- ACKNOWLEDGEMENT -- DISCUSSION -- REFERENCES -- Chapter 26. Oxidation-Reduction Reactions of 2,4,5-Triamino-6-hydroxypyrimidine and its Cofactor Activity in the Phenylalanine Hydroxylase System -- INTRODUCTION -- RESULTS -- DISCUSSION -- REFERENCES -- PART VII: HEME-CATALYZED REACTIONS OF OXYGEN AND PEROXIDES. , Chapter 27. Model Compound Studies Related to Peroxidases -- DISCUSSION -- REFERENCES -- Chapter 28. Identification of Polypeptide Environment of the Prosthetic Group of Hemoproteins -- ABSTRACT -- Chapter 29. A Comparison of Nitrosyl Myoglobin and the Model Compound N-Imidazole-Heme-NO: Differences in the Coupling of 14N to its Electronic Environment -- ABSTRACT -- PULSED EPR AND THE MODULATION EFFECT -- PROTONS AND DEUTERONS -- NITROGEN 14 -- THE THREE-PULSE ECHO SEQUENCE -- Cu (II)-INTERACTIONS WITH IMIDAZOLE -- MYOGLOBIN NITROXIDE AND 14N-IMIDAZOLE-HEME-NO -- THE EFFECT OF THE PROTEIN ON THE LIGAND BONDS -- DISCUSSION -- REFERENCES -- Chapter 30. Nuclear Magnetic Resonance Studies of Peroxidase and Catalase -- I. INTRODUCTION -- II. EXPERIMENTAL PROCEDURES -- III. RESULTS AND DISCUSSION -- IV. SUMMARY AND OUTLOOK -- ACKNOWLEDGMENTS -- DISCUSSION -- REFERENCES -- Chapter 31. Basic Isoenzymes of Horseradish Peroxidase -- I. PURIFICATION OF BASIC ISOENZYMES -- II. PROPERTIES AND COMPOSITIONS OF BASIC ISOENZYMES -- III. SUMMARY -- DISCUSSION -- REFERENCES -- Chapter 32. The Primary Structure of Yeast Cytochrome C Peroxidase -- REFERENCES -- Chapter 33. The Crystal Structure of Cytochrome c Peroxidase at 2.5 Å Resolution -- INTRODUCTION -- INTERPRETATION OF THE ELECTRON DENSITY MAP -- DESCRIPTION OF THE MODEL -- RELEVANCE TO CATALYTIC MECHANISM -- CCP-CYTOCHROME C COMPLEX -- ACKNOWLEDGEMENTS -- DISCUSSION -- REFERENCES -- Chapter 34. On the Past Eight Years of Peroxidase Research -- I. INTRODUCTION -- II. PRESENT STATE OF KNOWLEDGE -- DISCUSSION -- DISCUSSION -- REFERENCES -- Chapter 35. Modulation of Peroxidase-Dependent Reactions by Acid-Base Catalysis -- FORMATION OF COMPOUND I: THE ROLE OF ACID BASE CATALYSIS -- SELECTIVE MODIFICATION OF HRP -- DISCUSSION -- REFERENCES -- Chapter 36. Photodissociation Phenomena of NO-ferrihemoprotein Complexes. , 1. INTRODUCTION.