{"day":"01","publisher":"Elsevier","year":"2011","status":"public","page":"532 - 540","date_published":"2011-08-01T00:00:00Z","acknowledgement":"The work in authors’ laboratory was funded by the Medical Research Council.","month":"08","date_created":"2018-12-11T11:54:59Z","citation":{"ieee":"R. Efremov and L. A. Sazanov, “Respiratory complex I: ‘steam engine’ of the cell?,” Current Opinion in Structural Biology, vol. 21, no. 4. Elsevier, pp. 532–540, 2011.","mla":"Efremov, Rouslan, and Leonid A. Sazanov. “Respiratory Complex I: ‘steam Engine’ of the Cell?” Current Opinion in Structural Biology, vol. 21, no. 4, Elsevier, 2011, pp. 532–40, doi:10.1016/j.sbi.2011.07.002.","ama":"Efremov R, Sazanov LA. Respiratory complex I: “steam engine” of the cell? Current Opinion in Structural Biology. 2011;21(4):532-540. doi:10.1016/j.sbi.2011.07.002","short":"R. Efremov, L.A. Sazanov, Current Opinion in Structural Biology 21 (2011) 532–540.","apa":"Efremov, R., & Sazanov, L. A. (2011). Respiratory complex I: “steam engine” of the cell? Current Opinion in Structural Biology. Elsevier. https://doi.org/10.1016/j.sbi.2011.07.002","chicago":"Efremov, Rouslan, and Leonid A Sazanov. “Respiratory Complex I: ‘steam Engine’ of the Cell?” Current Opinion in Structural Biology. Elsevier, 2011. https://doi.org/10.1016/j.sbi.2011.07.002.","ista":"Efremov R, Sazanov LA. 2011. Respiratory complex I: ‘steam engine’ of the cell? Current Opinion in Structural Biology. 21(4), 532–540."},"quality_controlled":0,"title":"Respiratory complex I: 'steam engine' of the cell?","_id":"1974","doi":"10.1016/j.sbi.2011.07.002","author":[{"last_name":"Efremov","full_name":"Efremov, Rouslan G","first_name":"Rouslan"},{"orcid":"0000-0002-0977-7989","first_name":"Leonid A","full_name":"Leonid Sazanov","id":"338D39FE-F248-11E8-B48F-1D18A9856A87","last_name":"Sazanov"}],"abstract":[{"text":"Complex I is the first enzyme of the respiratory chain and plays a central role in cellular energy production. It has been implicated in many human neurodegenerative diseases, as well as in ageing. One of the biggest membrane protein complexes, it is an L-shaped assembly consisting of hydrophilic and membrane domains. Previously, we have determined structures of the hydrophilic domain in several redox states. Last year was marked by fascinating breakthroughs in the understanding of the complete structure. We described the architecture of the membrane domain and of the entire bacterial complex I. X-ray analysis of the larger mitochondrial enzyme has also been published. The core subunits of the bacterial and mitochondrial enzymes have remarkably similar structures. The proposed mechanism of coupling between electron transfer and proton translocation involves long-range conformational changes, coordinated in part by a long α-helix, akin to the coupling rod of a steam engine.","lang":"eng"}],"publication_status":"published","issue":"4","publication":"Current Opinion in Structural Biology","extern":1,"type":"journal_article","date_updated":"2021-01-12T06:54:27Z","publist_id":"5111","volume":21,"intvolume":" 21"}