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 Institute held at Edmonton, Alberta, Canada, August 13 – September 4, 1981: Nato Science Series C:, cartea 89
Editat de B.H. Dunford, D. Dolphin, K.N. Raymond, L. Siekeren Limba Engleză Hardback – 31 iul 1982
Toate formatele și edițiile | Preț | Express |
---|---|---|
Paperback (1) | 1207.43 lei 6-8 săpt. | |
SPRINGER NETHERLANDS – 22 noi 2011 | 1207.43 lei 6-8 săpt. | |
Hardback (1) | 1213.46 lei 6-8 săpt. | |
SPRINGER NETHERLANDS – 31 iul 1982 | 1213.46 lei 6-8 săpt. |
Din seria Nato Science Series C:
- 24% Preț: 797.66 lei
- 18% Preț: 941.47 lei
- 18% Preț: 940.99 lei
- 18% Preț: 1206.81 lei
- Preț: 389.76 lei
- Preț: 396.98 lei
- 18% Preț: 1218.43 lei
- 18% Preț: 1215.63 lei
- 18% Preț: 1210.98 lei
- 18% Preț: 1208.34 lei
- 18% Preț: 1804.16 lei
- 24% Preț: 1076.36 lei
- Preț: 383.93 lei
- Preț: 369.63 lei
- 18% Preț: 1211.60 lei
- Preț: 387.90 lei
- 18% Preț: 1205.54 lei
- 18% Preț: 1814.57 lei
- Preț: 393.19 lei
- Preț: 384.28 lei
- Preț: 390.88 lei
- Preț: 381.19 lei
- 18% Preț: 1817.38 lei
- 18% Preț: 935.10 lei
- 18% Preț: 1209.58 lei
- 18% Preț: 1215.63 lei
- Preț: 394.32 lei
- Preț: 399.45 lei
- 18% Preț: 1210.05 lei
- Preț: 411.33 lei
- 18% Preț: 1203.08 lei
Preț: 1213.46 lei
Preț vechi: 1479.84 lei
-18% Nou
Puncte Express: 1820
Preț estimativ în valută:
232.34€ • 241.94$ • 192.77£
232.34€ • 241.94$ • 192.77£
Carte tipărită la comandă
Livrare economică 14-28 februarie
Preluare comenzi: 021 569.72.76
Specificații
ISBN-13: 9789027714442
ISBN-10: 9027714444
Pagini: 536
Ilustrații: XIII, 415 p.
Dimensiuni: 155 x 235 x 34 mm
Greutate: 0.92 kg
Ediția:1982
Editura: SPRINGER NETHERLANDS
Colecția Springer
Seria Nato Science Series C:
Locul publicării:Dordrecht, Netherlands
ISBN-10: 9027714444
Pagini: 536
Ilustrații: XIII, 415 p.
Dimensiuni: 155 x 235 x 34 mm
Greutate: 0.92 kg
Ediția:1982
Editura: SPRINGER NETHERLANDS
Colecția Springer
Seria Nato Science Series C:
Locul publicării:Dordrecht, Netherlands
Public țintă
ResearchCuprins
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.