Copper-Containing Molecules

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Table of contents
  • Contentsv
  • Prefaceix
  • Chapter 1. Galactose Oxidase1
  • I. Introduction1
  • II. Protein Structure3
  • III. Sequence Correlations7
  • IV. The Metal-Binding Site11
  • V. Spectroscopic Probes of Metal Interactions17
  • VI. Probes of the Radical Site28
  • VII. The Free Radical-Coupled Copper Active Site36
  • VIII. Catalytic Mechanism37
  • IX. Cofactor Biogenesis41
  • X. Biomimetic Model Studies43
  • XI. Biomedical Applications44
  • XII. Summary and Conclusions46
  • References46
  • Chapter 2. Copper Metalloregulation of Gene Expression51
  • I. Copper Homeostasis51
  • II. Copper Metalloregulation in Prokaryotes53
  • III. Copper Metalloregulation in Eukaryotes57
  • IV. Copper-Induced Transcription in Animal Cells83
  • V. Summary of Mechanism of Copper-Modulated Transcription85
  • References87
  • Chapter 3. Bacterial Copper Transport93
  • I. Introduction93
  • II. The New Subclass of Heavy Metal CPx-type ATPases95
  • III. Copper Homeostasis in Enterococcus hirae102
  • IV. Copper Resistance in Escherichia coli107
  • V. Other Bacterial Copper ATPases110
  • VI. Mechanism of Copper ATPases114
  • VII. Other Copper-Resistance Systems114
  • VIII. Conclusions117
  • References119
  • Chapter 4. Understanding the Mechanism and Function of Copper P-type ATPases123
  • I. Introduction123
  • II. Heavy Metal Toxicity and Essentiality124
  • III. Vectorial Copper Transport125
  • IV. P-type ATPases127
  • V. Heavy Metal P-type ATPases129
  • VI. Conclusion145
  • References147
  • Chapter 5. Copper Chaperones151
  • I. Introduction151
  • II. Copper Chaperones of the Atxl-like Family161
  • III. Copper Chaperones for Copper-Zinc Superoxide Dismutase180
  • IV. Copper Chaperones for Cytochrome c Oxidase204
  • V. Conclusions210
  • References211
  • Chapter 6. Fet3p, Ceruloplasmin, and the Role of Copper in Iron Metabolism221
  • I. Copper Pumps, Ferroxidases, and Iron Homeostasis in Eukaryotes221
  • II. Biologic Copper Sites and the Multicopper Oxidases222
  • III. The Ferroxidases228
  • IV. Fet3p and Ftrlp in Iron Updake in Saccharomyces cerevisiae: The Molecular Link between Copper an238
  • V. Ferroxidase Structure: hCp and Fet3p240
  • VI. Ferroxidase Reaction246
  • VII. Convergence of Structural and Cell Biology in Iron Metabolism263
  • References265
  • Chapter 7. Blue Copper-Binding Domains271
  • I. lntroduction271
  • II. Four Classes of BCB Domain-Containing Proteins272
  • III. Folding Topology of the BCB Domains and Spectroscopic and Structural Properties of the Blue Cop282
  • IV. Cupredoxins288
  • V. Phytocyanins299
  • VI. Ephrins312
  • VII. Multicopper Oxidases312
  • VIII. Coagulation Factors V and VIII322
  • IX. BCB Domains with a Binuclear CuA Site329
  • X. Nitrosocyanin331
  • References333
  • Chapter 8. Cytochrome c Oxidase341
  • I. lntroduction341
  • II. Purification and Crystallization344
  • III. Composition of Bovine Heart Cytochrome c Oxidase348
  • IV. X-Ray Structures of Cytochrome c Oxidase351
  • V. Functions of the Redox-Active Metal Sites in This Enzyme358
  • VI. Proton Transfer Mechanism379
  • References392
  • Chapter 9. Nuclear Magnetic Resonance Spectroscopy Studies on Copper Proteins397
  • I. Introduction397
  • II. The Influence of the Copper Ion on the NMR Spectra398
  • III. Additional NMR Tools407
  • IV. NMR Studies on Mononuclear Type I Copper Proteins409
  • V. NMR Studies on Mononuclear Type II Copper-Containing Proteins425
  • VI. NMR Studies of Proteins Containing Polynuclear Copper Centers434
  • VII. Other Copper-Binding Proteins437
  • VIII. Perspectives440
  • References441
  • Author Index451
  • Subject Index483
Book details
  • Vendor Elsevier S & T
  • SKU 9780120342600
  • ISBN-13 9780080544069

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A wide range of researchers are currently investigating different properties and applications for copper-containing proteins. Biochemists researching metal metabolism in organisms ranging from bacteria to plants to animals are working in a completely different area of discovery than scientists studying the transportation and regulation of minerals and small molecule nutrients. They are both working with copper-containing proteins, but in very different ways and with differing anticipated outcomes.