The Biological Chemistry of Iron: A Look at the Metabolism of Iron and Its Subsequent Uses in Living Organisms Proceedings of the NATO Advanced Study

ISBN-13: 9789027714442 / Angielski / Twarda / 1982 / 415 str.

B. H. Dunford; D. Dolphin; K. N. Raymond

Opis

Proceedings of the NATO Advanced Study Institute, Edmonton, Alberta, Canada, August 23-September 4, 1981

Spis treści

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.