Copper-Containing Molecules (eBook)

Front Cover 1
Copper-Containing Proteins 4
Copyright Page 5
Contents 6
Preface 10
Chapter 1. Galactose Oxidase 12
I. Introduction 12
II. Protein Structure 14
III. Sequence Correlations 18
IV. The Metal-Binding Site 22
V. Spectroscopic Probes of Metal Interactions 28
VI. Probes of the Radical Site 39
VII. The Free Radical-Coupled Copper Active Site 47
VIII. Catalytic Mechanism 48
IX. Cofactor Biogenesis 52
X. Biomimetic Model Studies 54
XI. Biomedical Applications 55
XII. Summary and Conclusions 57
References 57
Chapter 2. Copper Metalloregulation of Gene Expression 62
I. Copper Homeostasis 62
II. Copper Metalloregulation in Prokaryotes 64
III. Copper Metalloregulation in Eukaryotes 68
IV. Copper-Induced Transcription in Animal Cells 94
V. Summary of Mechanism of Copper-Modulated Transcription 96
References 98
Chapter 3. Bacterial Copper Transport 104
I. Introduction 104
II. The New Subclass of Heavy Metal CPx-type ATPases 106
III. Copper Homeostasis in Enterococcus hirae 113
IV. Copper Resistance in Escherichia coli 118
V. Other Bacterial Copper ATPases 121
VI. Mechanism of Copper ATPases 125
VII. Other Copper-Resistance Systems 125
VIII. Conclusions 128
References 130
Chapter 4. Understanding the Mechanism and Function of Copper P-type ATPases 134
I. Introduction 134
II. Heavy Metal Toxicity and Essentiality 135
III. Vectorial Copper Transport 136
IV. P-type ATPases 138
V. Heavy Metal P-type ATPases 140
VI. Conclusion 156
References 158
Chapter 5. Copper Chaperones 162
I. Introduction 162
II. Copper Chaperones of the Atxl-like Family 172
III. Copper Chaperones for Copper-Zinc Superoxide Dismutase 191
IV. Copper Chaperones for Cytochrome c Oxidase 215
V. Conclusions 221
References 222
Chapter 6. Fet3p, Ceruloplasmin, and the Role of Copper in Iron Metabolism 232
I. Copper Pumps, Ferroxidases, and Iron Homeostasis in Eukaryotes 232
II. Biologic Copper Sites and the Multicopper Oxidases 233
III. The Ferroxidases 239
IV. Fet3p and Ftrlp in Iron Updake in Saccharomyces cerevisiae: The Molecular Link between Copper and Iron Metabolism 249
V. Ferroxidase Structure: hCp and Fet3p 251
VI. Ferroxidase Reaction 257
VII. Convergence of Structural and Cell Biology in Iron Metabolism 274
References 276
Chapter 7. Blue Copper-Binding Domains 282
I. lntroduction 282
II. Four Classes of BCB Domain-Containing Proteins 283
III. Folding Topology of the BCB Domains and Spectroscopic and Structural Properties of the Blue Copper Sites 293
IV. Cupredoxins 299
V. Phytocyanins 310
VI. Ephrins 323
VII. Multicopper Oxidases 323
VIII. Coagulation Factors V and VIII 333
IX. BCB Domains with a Binuclear CuA Site 340
X. Nitrosocyanin 342
References 344
Chapter 8. Cytochrome c Oxidase 352
I. lntroduction 352
II. Purification and Crystallization 355
III. Composition of Bovine Heart Cytochrome c Oxidase 359
IV. X-Ray Structures of Cytochrome c Oxidase 362
V. Functions of the Redox-Active Metal Sites in This Enzyme 369
VI. Proton Transfer Mechanism 390
References 403
Chapter 9. Nuclear Magnetic Resonance Spectroscopy Studies on Copper Proteins 408
I. Introduction 408
II. The Influence of the Copper Ion on the NMR Spectra 409
III. Additional NMR Tools 418
IV. NMR Studies on Mononuclear Type I Copper Proteins 420
V. NMR Studies on Mononuclear Type II Copper-Containing Proteins 436
VI. NMR Studies of Proteins Containing Polynuclear Copper Centers 445
VII. Other Copper-Binding Proteins 448
VIII. Perspectives 451
References 452
Author Index 462
Subject Index 494