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Mitochondrial function. Part A, Mitochondrial electron transport complexes and reactive oxygen species /
The first of two new volumes covering mitochondria, this volume examines modern methods that have been developed to examine mitochondrial electron transport chain complexes, iron-sulfur proteins and reactive oxygen species. The critically acclaimed laboratory standard for forty years, Methods in Enz...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | , |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
San Diego, California :
Academic Press/Elsevier,
�2009.
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| Edición: | 1. ed. |
| Colección: | Methods in enzymology ;
v. 456. |
| Temas: | |
| Acceso en línea: | Texto completo Texto completo Texto completo |
Tabla de Contenidos:
- Front Cover ; Methods in Enzymology: Mitochondrial Function, Part A: Mitochondrial Electron Transport Complexes and Reactive Oxygen Species; Copyright Page; Contents; Contributors; Preface; Methods in Enzymology; Chapter 1: Visualizing Functional Flexibility by Three-Dimensional Electron Microscopy: Reconstructing Complex I of the Mitochondrial Respiratory Chain; 1. Introduction; 2. Random Conical Reconstruction; 3. Application of the Techniques to Complex I From Yarrowia Lipolytica; 4. Conclusion; Acknowledgments; References.
- Chapter 2: Correlated Light and Electron Microscopy/Electron Tomography of Mitochondria in Situ 1. Introduction; 2. Light Microscopy; 3. Electron Microscope Tomography; Acknowledgments; References; Chapter 3: Studies of Complex I by Fourier Transform Infrared Spectroscopy; 1. Spectroscopic Studies of Complex I; 2. FTIR Difference Spectroscopy and Its Application to Complex I; 3. Preparation of Rehydrated Layers of Complex I for ATR-FTIR Spectroscopy; 4. Analysis of Rehydrated Complex I Layers by Perfusion-Induced ATR-FTIR Difference Spectroscopy.
- 5. Analysis of Rehydrated Complex I Layers by Electrochemically-Induced ATR-FTIR Difference Spectroscopy; 6. Model Compounds and Strategies for Interpretation; 7. Example IR Difference Spectra of Complex I; Acknowledgments; References; Chapter 4: Electron Transfer in Respiratory Complexes Resolved by an Ultra-Fast Freeze-Quench Approach; 1. Introduction; 2. Ultra-Fast Freeze-Quench Setup; 3. Sample Preparation; 4. Calibration of the Freeze-Quench Setup; 5. Application of Freeze-Quench Approach for the Monitoring of Complex I Reduction by NADH; References.
- Chapter 5: Use of Ruthenium Photooxidation Techniques to Study Electron Transfer in the Cytochrome bc1 Complex; 1. Introduction; 2. Design and Synthesis of Ruthenium-Labeled Proteins; 3. Measurement of Interprotein Electron Transfer in a Ruthenium-Labeled Protein; 4. Measurement of Electron Transfer between Ruz-39-Cc and Cytochrome bc1; 5. Measurement of Electron Transfer within the Cytochrome bc1 Complex; Acknowledgments; References; Chapter 6: Mass Spectrometric Characterization of the Thirteen Subunits of Bovine Respiratory Complexes that are Encoded in Mitochondrial DNA; 1. Introduction.
- 2. Analysis of Mitochondrial Membranes for mt-Proteins; 3. Analysis of Respiratory Complexes for mt-Proteins; 4. Mass Spectrometric Analysis of mt-Proteins; 5. Conclusions and Perspectives; References; Chapter 7: Tracing Human Mitochondrial Complex I Assembly by Use of GFP-Tagged Subunits; 1. Introduction; 2. Selection of Complex I Subunit for GFP Labeling; 3. Creation of Inducible Cell Line Expressing AcGFP1-tagged NDUFS3; 4. Tracing AcGFP1-Labeled NDUFS3 on BN-PAGE; Acknowledgments; References.