Oxidases and Related Redox Systems is a collection of papers from the Third International Symposium on Oxidases and Related Reduction Systems held in Albany, New York on July 3-7, 1979. This book deals with the oxygen and peroxide activating enzymes field. The book addresses electron transfer related to oxygen biochemistry by comparing quantum, semiclassical, and classical methods of electron transfer reactions. Several papers then discuss the active and toxic states of oxygen and superoxide as the discovery of superoxide dismutase activity of erythrocuprein can provide a means to studying oxygen reaction in biological systems. One paper then compares the active sites of molluskan and arthropodan hemocyanins, which are known as reversible oxygen-carriers. The result of this study is presented in a table. Other papers discuss the flavin catalyzed reactions of molecular oxygen and the implications of the physiological function of D-amino acid oxidase from inhibition studies. The book then explains the role of carbon monoxide in the reaction mechanism of oxygen with cytochrome oxidase. This collection will prove beneficial for research students and professors in the field of biochemistry and chemical physics.

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zlib/Science (General)/Tsso E. King, Howard S. Mason and Martin Morrison (Eds.)/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_2276624.pdf

International Symposium on Oxidases and Related Redox Systems (3rd 1979 State University of New York at Albany)

editors, Tsso E. King, Howard S. Mason, Martin Morrison

Tsoo E King; Howard S Mason; Martin Morrison

Woodhead Publishing Ltd

John Murray Press

Focal Press

United Kingdom and Ireland, United Kingdom

Elsevier Ltd., Oxford, 1982

First edition, Oxford, 1982

lg1107709

{"edition":"1","isbns":["0080244211","9780080244211"],"last_page":1235,"publisher":"Pergamon Press"}

类型: 图书

出版日期: 1982

出版社: Pergamon

摘要: ....One paper then compares the active sites of molluskan and arthropodan hemocyanins, which are...

Includes bibliographical references and index.

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 14 N-Imidazole-Heme-NO: Differences in the Coupling of 14 N 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 O 2 - 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 a 3 , 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 aa 3 : is there a proton-motive aa 3 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

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