A Look at the Metabolism of Iron and Its Subsequent Uses in Living Organisms Proceedings of the NATO Advanced Study Institute held at Edmonton, Alberta, Canada, August 13 ¿ September 4, 1981 Herausgegeben:Dunford, B. H.; Dolphin, D.; Raymond, K. N.; Sieker, L.
A Look at the Metabolism of Iron and Its Subsequent Uses in Living Organisms Proceedings of the NATO Advanced Study Institute held at Edmonton, Alberta, Canada, August 13 ¿ September 4, 1981 Herausgegeben:Dunford, B. H.; Dolphin, D.; Raymond, K. N.; Sieker, L.
The results of a NATO Advanced Study Institute (ASI) entitled "Coordination Chemistry Environments in Iron-Containing Proteins and Enzymes - Including Smaller Molecules and Model Systems" are summarized in this book. The ASI was held in the Province of Alberta, Canada, from August 23 to September 4, 1981. The first half of the conference was held on the campus of the University of Alberta, Edmonton, and the second half at the Overlander Lodge, Hinton. Two other conferences had the greatest impact upon the planning for this ASI. One was a NATO ASI held in Tomar, Portugal in September of 1979,…mehr
The results of a NATO Advanced Study Institute (ASI) entitled "Coordination Chemistry Environments in Iron-Containing Proteins and Enzymes - Including Smaller Molecules and Model Systems" are summarized in this book. The ASI was held in the Province of Alberta, Canada, from August 23 to September 4, 1981. The first half of the conference was held on the campus of the University of Alberta, Edmonton, and the second half at the Overlander Lodge, Hinton. Two other conferences had the greatest impact upon the planning for this ASI. One was a NATO ASI held in Tomar, Portugal in September of 1979, entitled "Metal Ions in Biology". Among the organizers for that conference were Allen Hill and Antonio Xavier; we are happy to acknowledge their beneficial influence on our subsequent conference. The other most influential conference was one organized by Ralph Wilkins and Dennis Darnell entitled "Methods for Determining Metal Ion Environments in Proteins" which was held in Las Cruces, New Mexico, U.S.A., January 10-12, 1979. The Las Cruces conference invited lectures were published as Volume 2 of "Advances in Inorganic Biochemistry", G. Eichhorn and L. Marzilli, editors.Hinweis: Dieser Artikel kann nur an eine deutsche Lieferadresse ausgeliefert werden.
Section A. Introduction.- Iron: An Element Well-Fitted for its Task?.- Substitution and Electron Transfer in Metal Complexes - Particularly those of Iron.- Oxidation States, Redox Potentials and Spin States.- Section B. Iron Metabolism.- Ferritin-the Structure and Function of an Iron Storage Protein.- Chemistry and Physiology of the Transferrins.- Coordination Chemistry of the Siderophores and Recent Studies of Synthetic Analogues.- Specificity of Siderophore Iron Uptake by Fungi.- Iron Uptake and Intracellular Iron Distribution in Cultured Rat Heart Cells: Effects of Iron Chelators.- Section C. Some Properties of the Cytochromes.- NMR Studies of Low-Spin Cytochromes.- Section D. Example of an Oxygen Carrier.- Substitution and Electron Transfer Processes in Hemerythrin.- The Environment of the Binuclear Iron Coordination Complex in Methemerythrin.- Section E. Iron-Sulfur Clusters and Enzymes.- Simple Iron-Sulfur Proteins: Methodology for Establishing the Type of Center.- Catalysis by Highly Active 12Fe-12S Containing Hydrogenases.- Hydrogenases: Physiology, Location and Relevance for Sulfate Reducing and Methane Forming Bacteria.- Generation, Transport and Transfer of Low-Potential Reducing Equivalents in Nitrogenase Catalysis.- Mössbauer and EPR Evidence on the Prosthetic Groups of the MoFe Protein.- Section F. Heme Model Systems.- Magnetic Complexities in Porphinatoiron(III) Complexes.- The Evaluation of Stabilization Energies (Empirical Resonance Energies) for Benzene, Porphine and [18] Annulene from Thermochemical Data and from AB Initio Calculations.- Models for Peroxidase and Cytochrome P-450 Enzymes.- Structure and Spectra of Stable and Transient States and Mechanisms of Oxidation of Model Cytochrome P-450.- Hemes of Hydroporphyrins.- Section G. Heme Enzymes.-Peroxidases.- The State of Protonation of the Proximal Histidyl Imidazole in Horseradish Peroxidase.- Coordination Characteristics of Proximal Histidine of Plant Peroxidases and their Relevance to the Heme-Linked Ionization.- Compounds I of Horseradish and Yeast Cytochrome C Peroxidases.- Cytochrome P450: Structure and States.- Cytochrome P450 as a Reductase and Oxene Transferase: Which is its Characteristic Function?.- Catalases and Iron-Porphyrin Model Systems: Roles of the Coordination Environment of Iron in Catalytic Mechanisms.- The Structure of Beef Liver Catalase.- The Subunits of Cytochrome C Oxidase.- Extended X-Ray Absorption Fine Structure of the Copper Sites in Cytochrome C Oxidase.- List of Participants.- Author Index.
Section A. Introduction.- Iron: An Element Well-Fitted for its Task?.- Substitution and Electron Transfer in Metal Complexes - Particularly those of Iron.- Oxidation States, Redox Potentials and Spin States.- Section B. Iron Metabolism.- Ferritin-the Structure and Function of an Iron Storage Protein.- Chemistry and Physiology of the Transferrins.- Coordination Chemistry of the Siderophores and Recent Studies of Synthetic Analogues.- Specificity of Siderophore Iron Uptake by Fungi.- Iron Uptake and Intracellular Iron Distribution in Cultured Rat Heart Cells: Effects of Iron Chelators.- Section C. Some Properties of the Cytochromes.- NMR Studies of Low-Spin Cytochromes.- Section D. Example of an Oxygen Carrier.- Substitution and Electron Transfer Processes in Hemerythrin.- The Environment of the Binuclear Iron Coordination Complex in Methemerythrin.- Section E. Iron-Sulfur Clusters and Enzymes.- Simple Iron-Sulfur Proteins: Methodology for Establishing the Type of Center.- Catalysis by Highly Active 12Fe-12S Containing Hydrogenases.- Hydrogenases: Physiology, Location and Relevance for Sulfate Reducing and Methane Forming Bacteria.- Generation, Transport and Transfer of Low-Potential Reducing Equivalents in Nitrogenase Catalysis.- Mössbauer and EPR Evidence on the Prosthetic Groups of the MoFe Protein.- Section F. Heme Model Systems.- Magnetic Complexities in Porphinatoiron(III) Complexes.- The Evaluation of Stabilization Energies (Empirical Resonance Energies) for Benzene, Porphine and [18] Annulene from Thermochemical Data and from AB Initio Calculations.- Models for Peroxidase and Cytochrome P-450 Enzymes.- Structure and Spectra of Stable and Transient States and Mechanisms of Oxidation of Model Cytochrome P-450.- Hemes of Hydroporphyrins.- Section G. Heme Enzymes.-Peroxidases.- The State of Protonation of the Proximal Histidyl Imidazole in Horseradish Peroxidase.- Coordination Characteristics of Proximal Histidine of Plant Peroxidases and their Relevance to the Heme-Linked Ionization.- Compounds I of Horseradish and Yeast Cytochrome C Peroxidases.- Cytochrome P450: Structure and States.- Cytochrome P450 as a Reductase and Oxene Transferase: Which is its Characteristic Function?.- Catalases and Iron-Porphyrin Model Systems: Roles of the Coordination Environment of Iron in Catalytic Mechanisms.- The Structure of Beef Liver Catalase.- The Subunits of Cytochrome C Oxidase.- Extended X-Ray Absorption Fine Structure of the Copper Sites in Cytochrome C Oxidase.- List of Participants.- Author Index.
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