I Iron-Sulfur Proteins (Non-mitochondrial electron transport proteins).- 1. Structure and Function of Chloroplast-Type Ferredoxins.- 2. Structural Investigations of the Environment of the Iron-Sulfur Cluster of the 2-Iron Ferredoxins.- 3. Studies on Bovine Adrenal Ferredoxin.- 4. Some Insight into Intramolecular Electron Transfer of an Adrenodoxin Molecule.- 5. Structural Studies of Electron Transport Proteins from Sulfate Reducing Bacteria: The Amino Acid Sequence of Two Rubredoxins Isolated from Desulfovibrio vulgaris and Desulfovibrio gigas.- 6. The Iron-Sulfur Centers and the Function of Hydrogenase from Clostridium pasteurianum.- 7. Sequence Investigation of the Clostridium pasteurianum Nitrogenase: The Partial Amino Acid Sequence of Azoferredoxin.- 8. On the Nature of an Intermediate that is Formed During the Enzymatic Conversion of Phenylalanine to Tyrosine.- 9. Some Properties of Bovine Pineal Tryptophan Hydroxylase.- 10. Evidence for Participation of NADH-Dependent Reductase in the Reaction of Benzoate 1,2-Dioxygenase (Benzoate Hydroxylase).- 11. Subunit Structure of Nonheme Iron-Containing Dioxygenases.- II Iron-Sulfur Proteins and Heme Proteins of the Mitochondrial Electron Transport System.- 12. Iron-Sulfur Proteins, the Most Numerous and Most Diversified Components of the Mitochondrial Electron Transfer System.- 13. Composition and Enzymatic Properties of the Mitochondrial NADH- and NADPH-Ubiquinone Reductase (Complex I).- 14. Factors Controlling the Turnover Number of Succinate Dehydrogenase: A New Look at an Old Problem.- 15. Biochemical and EPR Probes for Structure-Function Studies of Iron Sulfur Centers of Succinate Dehydrogenase.- 16. Heme a and Copper Environments in Cytochrome Oxidase'.- 17. Heme Interactions in Pseudomonas Cytochrome Oxidase.- III Other Heme and Non-Heme Fe-Proteins.- 18. Equilibrium States and Dynamic Reactions of Iron in the Camphor Monoxygenase System.- 19. Current Status of the Sequence Studies of the Pseudomonas putida Camphor Hydroxylase System.- 20. Highly Purified Cytochrome P-450 from Liver Microsomal Membranes: Recent Studies on the Mechanism of Catalysis.- 21. Characterization of Purified Cytochrome P-450scc and P-45011? from Bovine Adrenocortical Mitochondria.- 22. Purification and Properties of Cytochrome P-450 from Adrenocortical Mitochondria and Its Interaction with Adrenodoxin.- 23. The Role of Cytochrome P-450 in the Regulation of Steroid Biosynthesis.- 24. On the Participation of Cytochrome P-450 in the Mechanism of Prevention of Hepatic Carcinogenesis.- 25. Model System Studies of Axial Ligation in the Oxidized Reaction States of Cytochrome P-450 Enzymes.- 26. A New Assay Procedure for Indoleamine 2,3-Dioxygenase.- 27. Is Indoleamine 2,3-Dioxygenase Another Heme and Copper Containing Enzyme?.- 28. Copper Content of Indoleamine 2,3-Dioxygenase.- 29. Pseudomonad and Hepatic L-Tryptophan 2,3-Dioxygenase.- 30. On the Prosthetic Groups of L-Tryptophan 2,3-Dioxygenase from Pseudomonas: Evidence for Noninvolvement of Copper in the Reaction.- 31. The Search for Copper in L-Tryptophan 2,3-Dioxygenases.- 32. Comparison of Function of the Distal Base Between Myoglobin and Peroxidase.- 33. X-Ray Absorption Spectroscopy: Probing the Chemical and Electronic Structure of Metalloproteins.- 34. Carbonate: Key to Transferrin Chemistry.- IV Copper-Proteins.- 35. Oxidation and Reduction of Copper Ions in Catalytic Reactions of RHUS Laccase.- 36. Recent Studies on Copper Containing Oxidases.- 37. Collagen Cross-Linking: The Substrate Specificity of Lysyl Oxidase.- 38. Purification and Properties of Lung Lysyl Oxidase, a Copper-Enzyme.- 39. Binuclear Copper Clusters as Active Sites for Oxidases.- 40. An Interesting Reaction of Cupric Ions with Ferricyanide and Ferrocyanide.- 41. Formal Catalytic Mechanism of Ascorbate Oxidase.- 42. The Involvement of Superoxide and Trivalent Copper in the Galatose Oxidase Reaction.- 43. The Biological Role of Ceruloplasmin and Its Oxidase Activity.- 44. S
An Fe- and Cu-Protein Symposium was held on December 15-18, 1975 at the East West Center-University of Hawaii and was sponsored by the United States-Japan Cooperative Science Program under the auspices of the National Science Foundation and the Japan Society for the Promotion of Science. It was recognized by the organizers of the symposium that metalloproteins are very important in the field of health science and a subject worthy of discussion by experts from the United States, Japan and Europe. The meeting was restricted to Fe- and Cu-proteins but this is still a very broad subject matter and therefore, selected topics of current interest in this field were chosen. This book contains the collected papers from most of the symposium participants. The subject matter covered in this book is divided into four parts. These are: 1) the iron-sulfur proteins (which are not a part of the mitochondrial electron transport system); 2) the iron-sulfur proteins and heme proteins of the mitochondrial electron transport system; 3) other heme and nonheme iron proteins; and 5) selected copper proteins. The organizers of the symposium wish to express their gratitude to the participants, the session chairmen, and Drs. I.C. Gunsalus and E. Frieden who assisted in the organization of the symposium.
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