{"product_id":"mitochondrial-function-part-a-mitochondrial-electron-transport-complexes-and-reactive-oxygen-species-hardback-9780080877761","title":"Mitochondrial Function, Part A; Mitochondrial Electron Transport Complexes and Reactive Oxygen Species (Hardback) 9780080877761","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eMitochondrial Function, Part A\u003c\/font\u003e\u003cbr\u003e\r\n\u003cfont size=\"5\"\u003eMitochondrial Electron Transport Complexes and Reactive Oxygen Species\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cem\u003eThe first volume of Allison's two-volume treatment of Mitochondria describes new methods for charcterising mitochondrial electron transport complexes and reactive oxygen species.\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eWilliam S. Allison (Volume editor), Immo Scheffler (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780080877761, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 19 May 2009\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e502 pages\u003cbr\u003e22.9 x 15.1 x 3 cm, 1.06 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eThe first of two new volumes covering mitochondria, \u003ci\u003eMitochondrial Function, Part A\u003c\/i\u003e presents modern methods that have been developed to examine mitochondrial electron transport chain complexes, iron-sulfur proteins and reactive oxygen species. These new techniques provide investigators with sensitive, original approaches to the study of disease states associated with mitochondrial malfunction.\u003c\/p\u003e  \u003cp\u003eThe critically acclaimed laboratory standard for 40 years, \u003ci\u003eMethods in Enzymology\u003c\/i\u003e is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. With more than 400 volumes published, each \u003ci\u003eMethods in Enzymology\u003c\/i\u003e volume presents material that is relevant in today's labs -- truly an essential publication for researchers in all fields of life sciences.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003ePart A: Electron Transport Complexes\u003cbr\u003e1. Visualizing functional flexibility by three dimensional electron microscopy: reconstructing Complex I of the mitochondrial respiratory chain; M. Radermacher  \u003cbr\u003e2. Electron tomography of the mitochondrion; T. Frey, G. Perkins, M. Sun \u003cbr\u003e3. Mid-IR vibrational studies of complex I; D. Marshall, P. Rich \u003cbr\u003e4. Electron transfer in respiratory complexes resolved by an ultra-fast freeze-quench approach; N. Belevich, M. Verkhovskya, M. Verkhovsky \u003cbr\u003e5. Use of ruthenium photooxidation techniques to study electron transfer in the cytochrome bc1 complex; F. Millett, B. Durham, C. Yu, L. Yu \u003cbr\u003e6. Use of ruthenium photoreduction techniques to study electron transfer in cytochrome oxidase; F. Millett, B. Durham, R. Gennis   \u003cbr\u003e7. Mass spectrometric characterization of subunits of electron transfer complexes that are encoded in the mitochondrial genome; J. Carroll, J. Walker \u003cbr\u003e8. The assembly of respiratory chain complexes studied by GFP-tagged subunits, L. Nijtmans  \u003cbr\u003e9. Two-dimensional native electrophoresis for functional assays of mitochondrial complexes; W. Wittig, H. Schägger \u003cbr\u003e10. Reliable assay for complex I in human blood lymphocytes and skin fibroblasts; L. Elly, A. de Wit, W. Sluiter \u003cbr\u003e11. Purification of the cytochrome c reductase\/cytochrome c oxidase supercomplex of yeast mitochondria; E. Boekema and H. Braun \u003cbr\u003e12. Supercomplex organization of the yeast mitochondrial respiratory chain complexes and the ADP\/ATP carrier proteins; R. Stuart \u003cbr\u003e13. Role of cysteine desulfurase Nfs1 in human mitochondrial Fe-S protein biogenesis; O. Stehling, R. Lill \u003cbr\u003e14. Identification and properties of the novel 2Fe-2S center in the outer membrane protein, mitoNEET; S. Wiley, M. Rardin, J. Dixon  \u003cbr\u003e15. Nucleotide-dependent iron-sulfur cluster biogenesis in mitochondria; D. Pain \u003cbr\u003e16. Preparation of samples for EPR and Mössbauer spectroscopy of intact Saccharomyces cerrevisiae mitochondria; J. Garber-Morales, R. Miao, G. Holmes-Hampton, P. Lindahl\u003cbr\u003e17. Fluorescence correlation spectroscopy to probe mitochondrial mobility and intramatrix protein diffusion; P. Willems, W. Koopman\u003cbr\u003e18. Characterization of alternative complex I of Plasmodium falciparum mitochondria; N. Fisher, A.  J. Warman, S. Ward, G. Biagini\u003cbr\u003e19. Analysis of respiratory chain complex assembly using radiolabeled nuclear- and mitochondrial-encoded subunits; M. McKenzie, M. Lazarou, M. Ryan  \u003cbr\u003e\u003cbr\u003ePart B: Reactive Oxygen Species   \u003cbr\u003e20. Measuring redox changes to mitochondrial protein thiols using Redox DIGE; T. Hurd, K. Lilley, M. Murphy \u003cbr\u003e21.Measuring the effects of Hepatitis C proteins on mitochondrial electron transport and production of reactive oxygen species; S. Weinman\u003cbr\u003e22. Paraquat induced production of reactive oxygen species in brain mitochondria; D. Drechsel, M. Patel \u003cbr\u003e23. The uptake and interactions of the redox cycler paraquat with mitochondria; H. Cocheme; M. Murphy.\u003cbr\u003e24. Superoxide production by rat brain and skeletal muscle mitochondria; W. Kunz\u003cbr\u003e25. Quantitation, localization, and tissue specificities of mitochondrial reactive oxygen species production; C. Mathews\u003cbr\u003e26. The reaction mechanisms of electron transfer and superoxide generation in the cytochrome nc1 complex; D. Xia, S. Yang, Y. Yin, L. Yu; C.  Yu  \u003cbr\u003e27. Measurement of superoxide formation by mitochondrial complex I of Yarrowia lipolytica; S. Dröse, A. Galkin, U. Brandt \u003cbr\u003e28. An improved method for introducing point mutations into the mitochondrial cytochrme b gene to facilitate studying the role of cytochrome b in the formation of reactive oxygen species; B. Trumpower\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649097519384,"sku":"9780080877761","price":131.97,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780080877761_0953be7c-b826-4af8-b2eb-86074cdd6fd4.jpg?v=1695004010","url":"https:\/\/freshlyprintedbooks.co.uk\/products\/mitochondrial-function-part-a-mitochondrial-electron-transport-complexes-and-reactive-oxygen-species-hardback-9780080877761","provider":"Freshly Printed Books","version":"1.0","type":"link"}