Iron and Copper Proteins: Advances in Experimental Medicine and Biology, cartea 74
Editat de Kerry Yasunobuen Limba Engleză Paperback – 24 dec 2012
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Specificații
ISBN-13: 9781468432725
ISBN-10: 1468432729
Pagini: 612
Ilustrații: XI, 596 p.
Dimensiuni: 178 x 254 x 32 mm
Greutate: 1.05 kg
Ediția:Softcover reprint of the original 1st ed. 1976
Editura: Springer Us
Colecția Springer
Seria Advances in Experimental Medicine and Biology
Locul publicării:New York, NY, United States
ISBN-10: 1468432729
Pagini: 612
Ilustrații: XI, 596 p.
Dimensiuni: 178 x 254 x 32 mm
Greutate: 1.05 kg
Ediția:Softcover reprint of the original 1st ed. 1976
Editura: Springer Us
Colecția Springer
Seria Advances in Experimental Medicine and Biology
Locul publicării:New York, NY, United States
Public țintă
ResearchCuprins
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.- IIIOther 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 Propertiesof 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. Superoxide Dismutases: Studies of Structure and Mechanism.- 45. Iron- and Manganese-Containing Superoxide Dismutases: Structure, Distribution, and Evolutionary Relationships.- 46. Superoxide Dismutase in Photosynthetic Organisms.- 47. Chemistry and Biology of Copper-Chelatin.- 48. Circular Dichroism Study of Bovine Plasma Amine Oxidase, a Cu-Amine Oxidase.