Oxidases and Related Redox Systems. Proceedings of the Third International Symposium on Oxidases and Related Redox Systems, held in the State University of New York at Albany, USA

Content: 
Other Pergamon publications of related interest, Page ii
Front Matter, Page iii
Copyright, Page iv
PREFACE, Pages v-vi, Tsoo E. King, Howard S. Mason, Martin Morrison
On Quantum, Classical and Semiclassical Calculations of Electron Transfer Rates, Pages 3-19, R.A. Marcus
Theory of Ultrafast Electron Transfer in Bacterial Photosynthesis, Pages 21-33, Joshua Jortner
The Mechanism of Electron Transfer in the Electron Transport Chain, Pages 35-60, J.J. Hopfield
Outer Sphere Electron Transfer Between Iron Porphyrins, Pages 61-83, Ruth S. Wade, M.L. Chu, C.E. Castro
The Nature of the Primary Oxidants in Oxidations Mediated by Metal Ions, Pages 85-97, Cheves Walling
On the Question of Superoxide Toxicity and the Biological Function of Superoxide Dismutases, Pages 101-149, James A. Fee
Exacerbations of Oxygen Toxicity by Redox Active Compounds, Pages 151-167, H. Moustafa Hassan, Irwin Fridovich
Se and Non-Se Glutathione Peroxidases: Enzymology and Cell Physiology, Pages 169-189, Helmut Sies, Albrecht Wendel, Raymond F. Burk
Chemistry of Copper(III)-Peptide Complexes, Pages 193-206, Dale W. Margerum
Is Trivalent Copper a Viable Oxidation State in the Enzymatic Turnover of Copper Proteins?, Pages 207-224, W.E. Blumberg, J. Peisach, D.J. Kosman, H.S. Mason
Studies on the Mechanism of Action of the Copper(II) Enzyme, Galactose Oxidase, Pages 225-242, B. Marwedel, L. Kwiatkowski, D. Melnyk, P. Tressel, R.D. Bereman, R.J. Kurland, M.J. Ettinger, D.J. Kosman
Comparison of the Active Sites of Molluscan and Arthropodan Hemocyanins, Pages 245-261, Rene Lontie, Constant Gielens, Dominique Groeseneken, Jozef Verplaetse, Raphael Witters
Chemical and Spectroscopic Studies of the Binuclear Copper Active Site, Pages 263-290, Richard S. Himmelwright, Nancy C. Eickman, Aloysius F. Hepp, Edward I. Solomon
Hemocyanin Active Site Characterization by EXAFS and Resonance Raman Spectroscopy, Pages 291-304, T.G. Spiro, J.M. Brown, J.A. Larrabee, L. Powers, B. Kincaid
Reaction Inactivation of Tyrosinase, Pages 305-317, C. Dietler, K. Lerch
DT Diaphorase: Properties, Reaction Mechanism, Metabolic Function. A Progress Report, Pages 321-347, Christina Lind, Paul Hochstein, Lars Ernster
Transformations of Flavin and Pteridine Intermediates in Oxygen Transfer Models, Pages 349-378, H.I.X. Mager
The Role of the Apoprotein in Directing Pathways of Flavin Catalysis, Pages 379-405, P. Hemmerich, V. Massey
Lipid Environment of Monoamine Oxidase, Pages 407-421, Kunio Yagi, Makoto Naoi
4a-Peroxyflavins, Pages 423-446, Thomas C. Bruice
Implications Concerning the Physiological Function of D-Amino Acid Oxidase as Derived from Inhibition Studies, Pages 447-459, Gordon A. Hamilton, David J. Buckthal, Joseph Kalinyak
Resonance Raman Spectroscopic Studies of Non-heme-iron Dioxygenases, Pages 463-482, Thomas M. Loehr, William E. Keyes, Joann Sanders Loehr
Protocatechuate Dioxygenases: Structural and Mechanistic Studies, Pages 483-507, John D. Lipscomb, James B. Howard, John M. Wood
On the Mechanism of Lipoxygenase Catalysis, Pages 509-518, J.F.G. Vliegenthart, G.A. Veldink
Iron, an Essential Component of 4-Hydroxyphenylpyruvate Dioxygenase from Pseudomonas sp. Strain P.J. 874, Pages 519-542, Johanna Denum, Sven Lindstedt, Marianne Rundgren
Oxidation-Reduction Reactions of 2,4,5-Triamino-6-hydroxypyrimidine and its Cofactor Activity in the Phenylalanine Hydroxylase System, Pages 543-562, Seymour Kaufman, Lauraine Shaw-Goldstein
Model Compound Studies Related to Peroxidases, Pages 565-571, T.G. Traylor, T. Mincey, A. Berzinis, D. White
Identification of Polypeptide Environment of the Prosthetic Group of Hemoproteins, Page 573, M. Morrison
A Comparison of Nitrosyl Myoglobin and the Model Compound 14N-Imidazole-Heme-NO: Differences in the Coupling of 14N to its Electronic Environment, Pages 575-596, Jack Peisach
Nuclear Magnetic Resonance Studies of Peroxidase and Catalase, Pages 597-617, Isao Morishima, Satoshi Ogawa
Basic Isoenzymes of Horseradish Peroxidase, Pages 619-628, Y. Morita, S. Aibara, T. Kobayashi
The Primary Structure of Yeast Cytochrome C Peroxidase, Pages 629-638, Koji Takio, Koiti Titani, Lowell H. Ericsson, Takashi Yonetani
The Crystal Structure of Cytochrome c Peroxidase at 2.5 Å Resolution, Pages 639-652, Thomas L. Poulos, Stephen T. Freer, Richard A. Alden, Steven L. Edwards, Ulf Skoglund, Koji Takio, Nguyen-huu Xuong, Takashi Yonetani, Joseph Kraut
On the Past Eight Years of Peroxidase Research, Pages 653-670, H.B. Dunford, A.D. Nadezhdin
Modulation of Peroxidase-Dependent Reactions by Acid-Base Catalysis, Pages 671-684, Gregory R. Schonbaum
Photodissociation Phenomena of NO-ferrihemoprotein Complexes, Pages 685-702, Mamoru Tamura, Kazuo Kobayashi, Koichiro Hayashi, Hiroshi Hori
Acid-Base Groups and Function of Peroxidases, Pages 703-716, I. Yamazaki, Y. Hayashi, S. Kimura, T. Araiso, H. Yamada, R. Makino
The Role of Peroxide in the Functional Mechanism of Myeloperoxidase, Pages 717-732, John E. Harrison
Interaction of the Superoxide Radical With Peroxidase and with Other Iron Complexes, Pages 733-744, Barry Halliwell, Robert F. Pasternack, Johan de Rycker
Effect of Modification of Cys-149 On the Ligand Binding Properties of D-Glyceraldehyde-3-Phosphate Dehydrogenase, Pages 747-757, C.L. Tsou, K.Y. Zhao, Y.N. Lien, Y.S. Ho
The Components of Ubiquinol: Cytochrome c Oxidoreductase, Pages 759-783, E.C. Slater, C.A.M. Marres, S. de Vries, S.P.J. Albracht
Indoleamine 2, 3-Dioxygenase, Pages 787-809, Osamu Hayaishi
The Microsomal Electron Transport System Revisited: A New Look at Cytochrome P-450 Function, Pages 811-835, R.W. Estabrook, J. Werringloer, B.S.S. Masters, J.A. Peterson
The Chemical Basis of Mixed Function Oxidation, Pages 837-856, Stephen G. Sligar, David C. Pearson, Katherine A. Kennedy
Mechanistic Studies with Purified Liver Microsomal Cytochrome P-450: Comparison of O2 - and Peroxide-Supported Hydroxylation Reactions, Pages 857-885, M.J. Coon, R.E. White, R.C. Blake II
On the Mechanism of Action of Hepatic Cytochrome P-450 Reductase, Pages 887-901, Takashi Iyanagi, Howard S. Mason
Mechanism of Cholesterol Oxidation in NADPH-Dependent Microsomal Lipid Peroxidation System, Pages 903-918, Minoru Nakano, Katsuaki Sugioka
Metalloporphyrin Model Studies of Cytochrome c and Cytochrome Oxidase, Pages 921-936, W. Robert Scheidt, Christopher A. Reed
A Subunit of Cytochrome Oxidase which Contains Copper and Heme A, and has Spectroscopic Properties of Cytochrome a3, Pages 937-948, D.B. Winter, F.G. Foulke, H.S. Mason
Resolution of an Energy Coupling System into its Functional Components, Pages 949-969, D.E. Green, M. Fry, G. Blondin, H. Vande Zande
Effect of Phospholipid on EPR Visible Copper Signal of Cytochrome Oxidase, Pages 971-985, Yan-hui Wei, Tsoo E. King
Thermostable Single-Band Cytochrome Oxidase Capable of Energy Transformation in Liposomes, Pages 987-1004, Nobuhito Sone, Yasuo Kagawa
Fluorescence Labeling of Yeast Cytochrome c Oxidase, Pages 1005-1017, Michael E. Dockter
CYTOCHROME OXIDASE COMPOUND B AS A PEROXIDASE, Pages 1019-1035, Britton Chance, Patrick O'Connor, Esther Yang
The Relation between the Dipole Moment of Cytochrome c and the Activity with Cytochrome c Reductase and Cytochrome c Oxidase, Pages 1037-1053, W.H. Koppenol, S. Ferguson-Miller, N. Osheroff, S.H. Speck, E. Margoliash
The Reaction Between Cytochrome c and Cytochrome c Oxidase, Pages 1055-1065, B.F. van Gelder, J. Wilms, E.C.I. Veerman
Further Studies of an Intermediate in the Oxidation of Reduced Cytochrome c Oxidase by Oxygen, Pages 1067-1088, Helmut Beinert, Robert W. Shaw, W. Richard Dunham, Richard H. Sands
The Mechanism of Dioxygen Reduction in Cytochrome c Oxidase and Laccase, Pages 1089-1118, Bo G. Malmström
The Oxygen Concentration Dependence of Cytochrome c Oxidase in Oxidative Phosphorylation, Pages 1119-1137, David F. Wilson, Maria Erecinska, Steven Sandler, David Nelson
Activation of Cytochrome-c-Oxidase, Pages 1139-1147, M. Brunori, A. Colosimo, P. Sarti, E. Antonini, W. Lalla-Maharajh, M.T. Wilson
Scalar and vectorial pH effects in cytochrome aa3: is there a proton-motive aa3 cycle?, Pages 1149-1160, Peter Nicholls, John M. Wrigglesworth
Carbon Monoxide - Ancient and Modern Clue to the Reaction Mechanism of Oxygen with Cytochrome Oxidase, Pages 1161-1179, Peter Nicholls
Significance of Temperature-Dependent Conformers of Cytochrome Oxidase in Reaction with Electron Donors and Ligands, Pages 1181-1200, Yutaka Orii, Toshiaki Miki
Analysis of Proton Transfer Reactions in the Cytochrome-C-Oxidase of Mitochondria, Pages 1201-1224, S. Papa, F. Guerrieri, M. Lorusso, G. Izzo, F. Capuano, D. Boffoli
Some Comments on the Protonmotive Q Cycle, Pages 1225-1246, Peter Mitchell
A Critique of ←H+/2e− and →e−/2e− Measurements, Pages 1247-1268, Peter Mitchell
INDEX, Pages 1269-1282