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.
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 Se...
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Full text |
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Personal Name(s): | Dolphin, David, editor |
Dunford, H. Brian, editor / Raymond, Kenneth N., editor / Sieker, Larry, editor | |
Imprint: |
Dordrecht :
Springer,
1982
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Physical Description: |
XIII, 415 p. online resource. |
Note: |
englisch |
ISBN: |
9789400978829 |
DOI: |
10.1007/978-94-009-7882-9 |
Series Title: |
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NATO Advanced Study Institutes Series, Series C — Mathematical and Physical Sciences ;
89 |
Subject (LOC): |
- 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.