The Biological Chemistry of Iron [E-Book] : 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 / edited by H. Brian Dunford, David Dolphin, Kenneth N. Raymond, Larry Sieker.
Dolphin, David, (editor)
Dunford, H. Brian, (editor) / Raymond, Kenneth N., (editor) / Sieker, Larry, (editor)
Dordrecht : Springer, 1982
XIII, 415 p. online resource.
englisch
9789400978829
10.1007/978-94-009-7882-9
NATO Advanced Study Institutes Series, Series C — Mathematical and Physical Sciences ; 89
Full Text
Table of Contents:
  • 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.