Valentine / Gralla Copper-Containing Molecules

1. Auflage 2002
ISBN: 978-0-08-054406-9
Verlag: Elsevier Science & Techn.
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, Band Volume 60, 493 Seiten, Web PDF

Reihe: Advances in Protein Chemistry

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.

Autoren/Hrsg.

Valentine, Joan S.

Gralla, Edith B.

Inhaltsverzeichnis

1;Front Cover;1
2;Copper-Containing Proteins;4
3;Copyright Page;5
4;Contents;6
5;Preface;10
6;Chapter 1. Galactose Oxidase;12
6.1;I. Introduction;12
6.2;II. Protein Structure;14
6.3;III. Sequence Correlations;18
6.4;IV. The Metal-Binding Site;22
6.5;V. Spectroscopic Probes of Metal Interactions;28
6.6;VI. Probes of the Radical Site;39
6.7;VII. The Free Radical-Coupled Copper Active Site;47
6.8;VIII. Catalytic Mechanism;48
6.9;IX. Cofactor Biogenesis;52
6.10;X. Biomimetic Model Studies;54
6.11;XI. Biomedical Applications;55
6.12;XII. Summary and Conclusions;57
6.13;References;57
7;Chapter 2. Copper Metalloregulation of Gene Expression;62
7.1;I. Copper Homeostasis;62
7.2;II. Copper Metalloregulation in Prokaryotes;64
7.3;III. Copper Metalloregulation in Eukaryotes;68
7.4;IV. Copper-Induced Transcription in Animal Cells;94
7.5;V. Summary of Mechanism of Copper-Modulated Transcription;96
7.6;References;98
8;Chapter 3. Bacterial Copper Transport;104
8.1;I. Introduction;104
8.2;II. The New Subclass of Heavy Metal CPx-type ATPases;106
8.3;III. Copper Homeostasis in Enterococcus hirae;113
8.4;IV. Copper Resistance in Escherichia coli;118
8.5;V. Other Bacterial Copper ATPases;121
8.6;VI. Mechanism of Copper ATPases;125
8.7;VII. Other Copper-Resistance Systems;125
8.8;VIII. Conclusions;128
8.9;References;130
9;Chapter 4. Understanding the Mechanism and Function of Copper P-type ATPases;134
9.1;I. Introduction;134
9.2;II. Heavy Metal Toxicity and Essentiality;135
9.3;III. Vectorial Copper Transport;136
9.4;IV. P-type ATPases;138
9.5;V. Heavy Metal P-type ATPases;140
9.6;VI. Conclusion;156
9.7;References;158
10;Chapter 5. Copper Chaperones;162
10.1;I. Introduction;162
10.2;II. Copper Chaperones of the Atxl-like Family;172
10.3;III. Copper Chaperones for Copper-Zinc Superoxide Dismutase;191
10.4;IV. Copper Chaperones for Cytochrome c Oxidase;215
10.5;V. Conclusions;221
10.6;References;222
11;Chapter 6. Fet3p, Ceruloplasmin, and the Role of Copper in Iron Metabolism;232
11.1;I. Copper Pumps, Ferroxidases, and Iron Homeostasis in Eukaryotes;232
11.2;II. Biologic Copper Sites and the Multicopper Oxidases;233
11.3;III. The Ferroxidases;239
11.4;IV. Fet3p and Ftrlp in Iron Updake in Saccharomyces cerevisiae: The Molecular Link between Copper and Iron Metabolism;249
11.5;V. Ferroxidase Structure: hCp and Fet3p;251
11.6;VI. Ferroxidase Reaction;257
11.7;VII. Convergence of Structural and Cell Biology in Iron Metabolism;274
11.8;References;276
12;Chapter 7. Blue Copper-Binding Domains;282
12.1;I. lntroduction;282
12.2;II. Four Classes of BCB Domain-Containing Proteins;283
12.3;III. Folding Topology of the BCB Domains and Spectroscopic and Structural Properties of the Blue Copper Sites ;293
12.4;IV. Cupredoxins;299
12.5;V. Phytocyanins;310
12.6;VI. Ephrins;323
12.7;VII. Multicopper Oxidases;323
12.8;VIII. Coagulation Factors V and VIII;333
12.9;IX. BCB Domains with a Binuclear CuA Site;340
12.10;X. Nitrosocyanin;342
12.11;References;344
13;Chapter 8. Cytochrome c Oxidase;352
13.1;I. lntroduction;352
13.2;II. Purification and Crystallization;355
13.3;III. Composition of Bovine Heart Cytochrome c Oxidase;359
13.4;IV. X-Ray Structures of Cytochrome c Oxidase;362
13.5;V. Functions of the Redox-Active Metal Sites in This Enzyme;369
13.6;VI. Proton Transfer Mechanism;390
13.7;References;403
14;Chapter 9. Nuclear Magnetic Resonance Spectroscopy Studies on Copper Proteins;408
14.1;I. Introduction;408
14.2;II. The Influence of the Copper Ion on the NMR Spectra;409
14.3;III. Additional NMR Tools;418
14.4;IV. NMR Studies on Mononuclear Type I Copper Proteins;420
14.5;V. NMR Studies on Mononuclear Type II Copper-Containing Proteins;436
14.6;VI. NMR Studies of Proteins Containing Polynuclear Copper Centers;445
14.7;VII. Other Copper-Binding Proteins;448
14.8;VIII. Perspectives;451
14.9;References;452
15;Author Index;462
16;Subject Index;494