Fe-S Cluster Enzymes Part A: Methods in Enzymology, cartea 595
Sheila S. Daviden Limba Engleză Hardback – sep 2017
- Contain contributions from leading authorities on enzymology
- Informs and updates on all the latest developments in the field
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Specificații
ISBN-13: 9780128119440
ISBN-10: 0128119446
Pagini: 442
Dimensiuni: 152 x 229 x 27 mm
Editura: ELSEVIER SCIENCE
Seria Methods in Enzymology
ISBN-10: 0128119446
Pagini: 442
Dimensiuni: 152 x 229 x 27 mm
Editura: ELSEVIER SCIENCE
Seria Methods in Enzymology
Public țintă
Biochemists, biophysicists, molecular biologists, analytical chemists, and physiologistsCuprins
1. De Novo Design of Iron–Sulfur Proteins
Zahra B. Dizicheh, Nicholas Halloran, William Asma and Giovanna Ghirlanda
2. In Vitro Studies of Cellular Iron–Sulfur Cluster Biosynthesis, Trafficking, and Transport
Christine Wachnowsky and J.A. Cowan
3. A Polymerase With Potential: The Fe–S Cluster in Human DNA Primase
Marilyn E. Holt, Lauren E. Salay and Walter J. Chazin
4. Combined Biochemical, Biophysical, and Cellular Methods to Study Fe–S Cluster Transfer and Cytosolic Aconitase Repair by MitoNEET
Cécile Mons, Ioana Ferecatu, Sylvie Riquier, Ewen Lescop, Cécile Bouton and Marie-Pierre Golinelli-Cohen
5. Defining the Architecture of the Core Machinery for the Assembly of Fe–S Clusters in Human Mitochondria
O. Gakh, W. Ranatunga, B.K. Galeano, D.S. Smith IV, J.R. Thompson and G. Isaya
6. Fe–S Cluster Hsp70 Chaperones: The Atpase Cycle and Protein Interactions
Rafal Dutkiewicz, Malgorzata Nowak, Elizabeth A. Craig and Jaroslaw Marszalek
7. B. subtilis as a Model for Studying the Assembly of Fe–S Clusters in Gram-Positive Bacteria
Patricia C. Dos Santos
8. Genetic, Biochemical, and Biophysical Methods for Studying Fe–S Proteins and Their Assembly
S. Ollagnier-de Choudens and F. Barras
9. Structural Characterization of Poised States in the Oxygen Sensitive Hydrogenases and Nitrogenases
Jacob H. Artz, Oleg A. Zadvornyy, David W. Mulder, Paul W. King and John W. Peters
10. Nitrogenase Assembly: Strategies and Procedures
Nathaniel S. Sickerman, Yilin Hu and Markus W. Ribbe
11. TsrM as a Model for Purifying and Characterizing Cobalamin-Dependent Radical S-Adenosylmethionine Methylases
Anthony J. Blaszczyk, Roy X. Wang and Squire J. Booke
12. Mechanism-Based Strategies for Structural Characterization of Radical SAM Reaction Intermediates
K.M. Davis and A.K. Boal
Zahra B. Dizicheh, Nicholas Halloran, William Asma and Giovanna Ghirlanda
2. In Vitro Studies of Cellular Iron–Sulfur Cluster Biosynthesis, Trafficking, and Transport
Christine Wachnowsky and J.A. Cowan
3. A Polymerase With Potential: The Fe–S Cluster in Human DNA Primase
Marilyn E. Holt, Lauren E. Salay and Walter J. Chazin
4. Combined Biochemical, Biophysical, and Cellular Methods to Study Fe–S Cluster Transfer and Cytosolic Aconitase Repair by MitoNEET
Cécile Mons, Ioana Ferecatu, Sylvie Riquier, Ewen Lescop, Cécile Bouton and Marie-Pierre Golinelli-Cohen
5. Defining the Architecture of the Core Machinery for the Assembly of Fe–S Clusters in Human Mitochondria
O. Gakh, W. Ranatunga, B.K. Galeano, D.S. Smith IV, J.R. Thompson and G. Isaya
6. Fe–S Cluster Hsp70 Chaperones: The Atpase Cycle and Protein Interactions
Rafal Dutkiewicz, Malgorzata Nowak, Elizabeth A. Craig and Jaroslaw Marszalek
7. B. subtilis as a Model for Studying the Assembly of Fe–S Clusters in Gram-Positive Bacteria
Patricia C. Dos Santos
8. Genetic, Biochemical, and Biophysical Methods for Studying Fe–S Proteins and Their Assembly
S. Ollagnier-de Choudens and F. Barras
9. Structural Characterization of Poised States in the Oxygen Sensitive Hydrogenases and Nitrogenases
Jacob H. Artz, Oleg A. Zadvornyy, David W. Mulder, Paul W. King and John W. Peters
10. Nitrogenase Assembly: Strategies and Procedures
Nathaniel S. Sickerman, Yilin Hu and Markus W. Ribbe
11. TsrM as a Model for Purifying and Characterizing Cobalamin-Dependent Radical S-Adenosylmethionine Methylases
Anthony J. Blaszczyk, Roy X. Wang and Squire J. Booke
12. Mechanism-Based Strategies for Structural Characterization of Radical SAM Reaction Intermediates
K.M. Davis and A.K. Boal