Copper-containing proteins /

Preface p. ix
Galactose Oxidase James W. Whittaker
I. Introduction p. 1
II. Protein Structure p. 3
III. Sequence Correlations p. 7
IV. The Metal-Binding Site p. 11
V. Spectroscopic Probes of Metal Interactions p. 17
VI. Probes of the Radical Site p. 28
VII. The Free Radical-Coupled Copper Active Site p. 36
VIII. Catalytic Mechanism p. 37
IX. Cofactor Biogenesis p. 41
X. Biomimetic Model Studies p. 43
XI. Biomedical Applications p. 44
XII. Summary and Conclusions p. 46
References p. 46
Copper Metalloregulation of Gene Expression Dennis R. Winge
I. Copper Homeostasis p. 51
II. Copper Metalloregulation in Prokaryotes p. 53
III. Copper Metalloregulation in Eukaryotes p. 57
IV. Copper-Induced Transcription in Animal Cells p. 83
V. Summary of Mechanism of Copper-Modulated Transcription p. 85
Reference p. 87
Bacterial Copper Transport Zen Huat Lu and Marc Solioz
I. Introduction p. 93
II. The New Subclass of Heavy Metal CPx-type ATPases p. 95
III. Copper Homeostasis in Enterococcus hirae p. 102
IV. Copper Resistance in Escherichia coli p. 107
V. Other Bacterial Copper ATPases p. 110
VI. Mechanism of Copper ATPases p. 114
VII. Other Copper-Resistance Systems p. 114
VIII. Conclusions p. 117
References p. 119
Understanding the Mechanism and Function of Copper P-type ATPases Ilia Voskoboinik and James Camakaris and Julian F. B. Mercer
I. Introduction p. 123
II. Heavy Metal Toxicity and Essentiality p. 124
III. Vectorial Copper Transport p. 125
IV. P-type ATPases p. 127
V. Heavy Metal P-type ATPases p. 129
VI. Conclusion p. 145
References p. 147
Copper Chaperones Jennifer Stine Elam and Susan T. Thomas and Stephen P. Holloway and Alexander B. Taylor and P. John hart
I. Introduction p. 151
II. Copper Chaperones of the Atxl-like Family p. 161
III. Copper Chaperones for Copper-Zinc Superoxide Dismutase p. 180
IV. Copper Chaperones for Cytochrome c Oxidase p. 204
V. Conclusions p. 210
References p. 211
Fet3p, Ceruloplasmin, and the Role of Copper in Iron Metabolism Daniel J. Kosman
I. Copper Pumps, Ferroxidases, and Iron Homeostasis in Eukaryotes p. 221
II. Biologic Copper Sites and the Multicopper Oxidases p. 222
III. The Ferroxidases p. 228
IV. Fet3p and Ftr1p in Iron Updake in Saccharomyces cerevisiae: The Molecular Link between Copper and Iron Metabolism p. 238
V. Ferroxidase Structure: hCp and Fet3p p. 240
VI. Ferroxidase Reaction p. 246
VII. Convergence of Structural and Cell Biology in Iron Metabolism p. 263
References p. 265
Blue Copper-Binding Domains Aram M. Nersissian and Eric L. Shipp
I. Introduction p. 271
II. Four Classes of BCB Domain-Containing Proteins p. 272
III. Folding Topology of the BCB Domains and Spectroscopic and Structural Properties of the Blue Copper Sites p. 282
IV. Cupredoxins p. 288
V. Phytocyanins p. 299
VI. Ephrins p. 312
VII. Multicopper Oxidases p. 312
VIII. Coagulation Factors V and VIII p. 322
IX. BCB Domains with a Binuclear CuA Site p. 329
X. Nitrosocyanin p. 331
References p. 333
Cytochrome c Oxidase Shinya Yoshikawa
I. Introduction p. 341
II. Purification and Crystallization p. 344
III. Composition of Bovine Heart Cytochrome c Oxidase p. 348
IV. X-Ray Structures of Cytochrome c Oxidase p. 351
V. Functions of the Redox-Active Metal Sites in This Enzyme p. 358
VI. Proton Transfer Mechanism p. 379
References p. 392
Nuclear Magnetic Resonance Spectroscopy Studies on Copper Proteins Lucia Banci and Roberta Pierattelli and Alejandro J. Vila
I. Introduction p. 397
II. The Influence of the Copper Ion on the NMR Spectra p. 398
III. Additional NMR Tools p. 407
IV. NMR Studies on Mononuclear Type I Copper Proteins p. 409
V. NMR Studies on Mononuclear Type II Copper-Containing Proteins p. 425
VI. NMR Studies of Proteins Containing Polynuclear Copper Centers p. 434
VII. Other Copper-Binding Proteins p. 437
VIII. Perspectives p. 440
References p. 441
Author Index p. 451
Subject Index p. 483