K. D. Karlin, Z. Tyeklar

Bioinorganic Chemistry of Copper (eBook, PDF)

• Format: PDF

Produktbeschreibung

Bioinorganic Chemistry of Copper focuses on the vital role of copper ions in biology, especially as an essential metalloenzyme cofactor. The book is highly interdisciplinary in its approach--the outstanding list of contributors includes coordination chemists, biochemists, biophysicists, and molecular biologists. Chapters are grouped into major areas of research interest in inorganic copper chemistry, spectroscopy, oxygen chemistry, biochemistry, and molecular biology. The book also discusses basic research of great potential importance to pharmaceutical scientists. This book is based on the first Johns Hopkins University Copper Symposium, held in August 1992. Researchers in chemistry, biochemistry, molecular biology, and medicinal chemistry will find it to be an essential reference on its subject.

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Produktdetails

• Verlag: Springer Netherlands
• Seitenzahl: 506
• Erscheinungstermin: 6. Dezember 2012
• Englisch
• ISBN-13: 9789401168755
• Artikelnr.: 44183437

Inhaltsangabe

Copper Proteins and Complex Spectroscopy.- 1. Electronic Structures of Active Sites in Copper Proteins: Coupled Binuclear and Trinuclear Cluster Sites.- 2. Pulsed EPR Studies of Copper Proteins.- 3. Copper(II) Complexes of Binucleating Maciocyclic Bis(disulfide) Tetramine Ligands.- "Blue" Copper Proteins and Electron Transfer.- 4. Investigation of Type 1 Copper Site Geometry by Spectroscopy and Molecular Redesign.- 5. Metalloprotein Ligand Redesign: Characterization of Copper-Cysteinate Proteins Derived from Yeast Copper-Zinc Superoxide Dismutase.- 6. Electron Transfer Reactivity of Mutants of the Blue Copper Protein Plastocyanin.- 7. Studies of CNI Copper Coordination Compounds: What Determines the Electron-Transfer Rate of the Blue-Copper Proteins?.- Natural and Synthetic Regulation of Gene Expression.- 8. Chemical and Genetic Studies of Copper Resistance in E. coli.- 9. Cuprous-Thiolate Polymetalic Clusters in Biology.- 10. Mechanisms of Copper Ion Homeostasis in Yeast.- 11. RNA Hydrolysis by Cu(II) Complexes: Toward Synthetic Ribonucleases and Ribozymes.- Hemocyanin and Copper Monooxygenases.- 12. Three-Dimensional Structure of the Oxygenated Form of the Hemocyanin Subunit II of Limulus polyphemus at Atomic Resolution.- 13. New Probes of Oxygen Binding and Activation: Application to Dopamine ?-Monooxygenase.- 14. Chemical and Spectroscopic Studies on Dopamine ?-Hydroxylase and Other Copper Monooxygenases.- 15. The Copper Ions in the Membrane-Associated Methane Monooxygenase.- 16. The Enzymology of Peptide Amidation.- Copper-Mediated Redox/Oxidative Pathways.- 17. Redox Decomposition Reactions of Copper(III) Peptide Complexes.- 18. Free Radical Induced Cleavage of Organic Molecules Catalyzed by Copper Ions - An Alternative Pathway for Biological Damage.- 19.Copper-Mediated Nitrogen Ligand Oxidation and Oxygenation.- Dioxygen-Binding and Oxygenation Reactions.- 20. Synthesis, Structure and Properties of ?-?2:?2 Peroxo Dinuclear Copper complexes Modeling the Active Site of Oxyhemocyanin and Oxytyrosinase.- 21. Kinetics and Mechanisms of Cu(I)/O2 Reactions.- 22. Functional Models for Hemocyanin and Copper Monooxygenases.- 23. Dioxygen Activation by Biomimetic Dinuclear Complexes.- 24. Oxidation Catalysis; A Dinuclear Approach.- 25. Dioxygen Activation and Transport by Dinuclear Copper(I) Macrocyclic Complexes.- 26. Imidazole-Ligated Copper Complexes: Synthesis, Structure, and Reactivity.- 27. Oxidation of Unactivated Hydrocarbons: Models for Tyrosinase and Dopamine ?-Hydroxylase.- 28. Copper-Pteridine Chemistry. Structures, Properties, and Phenylalanine Hydroxylase Models.- 29. Design and Synthesis of Model Systems for Dioxygen Binding and Activation in Dinuclear Copper Proteins.- 30. Copper Dioxygenation Chemistry Relevant to Quercetin Dioxygenase.- Nitrogen Oxide (NOx) Chemistry and Biochemistry.- 31. Two Crystal Forms of A. cycloclastes Nitrite Reductase.- 32. Characterization of Mononuclear Copper-Nitrogen Oxide Complexes: Models of NOx Binding to Isolated Active Sites in Copper Proteins.- 33. The EPR-Detectable Copper of Nitrous Oxide Reductase as a Model for CuA in Cytochrome c Oxidase: A Multifrequency Electron Paramagnetic Resonance Investigation.- 34. Mixed-Ligand, NON-Nitrosyl Cu(II) Complexes As Potential Pharmacological Agents via NO Release.- Copper Oxidases.- 35. Copper-Containing Enzymes: Structure and Mechanism.- 36. Active Site Ligand Interactions in Galactose Oxidase.- 37. Structure and Reactivity of Copper-Containing Amine Oxidases.- 38. Ascorbate Oxidase Structure and Chemistry.- 39. Cytochrome cOxidase: A Brief Introduction and Some New Results from High Field ENDOR Studies of the CuA and CuB Sites.

Rezensionen

Good bibliographies accompany each article. A book for the reference shelf of any laboratory group working with bioinorganic copper - Chemical Monographs Review; Summarizing the book may be a variable asset for those working or considering starting in biological copper research, as it gives a pretty complete review of current developments in the field - Molecular Biology Reports; This book provides an intriguing insight of current expertise in the Bioinorganic chemistry of copper - ioinorganic Chemistry of Copper; Good bibliographies accompany each article. A book for the reference shelf of any laboratory group working with bioinorganic copper - Chemical Monographs Review; Good bibliographies accompany each article. A book for the reference shelf of any laboratory group working with bioinorganic copper - Chemical Monographs Review