{"day":"01","publisher":"Elsevier","month":"07","year":"2008","intvolume":" 1777","citation":{"apa":"Morgan, D., & Sazanov, L. A. (2008). Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides. Biochimica et Biophysica Acta - Bioenergetics. Elsevier. https://doi.org/10.1016/j.bbabio.2008.03.023","ista":"Morgan D, Sazanov LA. 2008. Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides. Biochimica et Biophysica Acta - Bioenergetics. 1777(7–8), 711–718.","chicago":"Morgan, David, and Leonid A Sazanov. “Three-Dimensional Structure of Respiratory Complex I from Escherichia Coli in Ice in the Presence of Nucleotides.” Biochimica et Biophysica Acta - Bioenergetics. Elsevier, 2008. https://doi.org/10.1016/j.bbabio.2008.03.023.","ama":"Morgan D, Sazanov LA. Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides. Biochimica et Biophysica Acta - Bioenergetics. 2008;1777(7-8):711-718. doi:10.1016/j.bbabio.2008.03.023","ieee":"D. Morgan and L. A. Sazanov, “Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides,” Biochimica et Biophysica Acta - Bioenergetics, vol. 1777, no. 7–8. Elsevier, pp. 711–718, 2008.","short":"D. Morgan, L.A. Sazanov, Biochimica et Biophysica Acta - Bioenergetics 1777 (2008) 711–718.","mla":"Morgan, David, and Leonid A. Sazanov. “Three-Dimensional Structure of Respiratory Complex I from Escherichia Coli in Ice in the Presence of Nucleotides.” Biochimica et Biophysica Acta - Bioenergetics, vol. 1777, no. 7–8, Elsevier, 2008, pp. 711–18, doi:10.1016/j.bbabio.2008.03.023."},"extern":1,"date_published":"2008-07-01T00:00:00Z","quality_controlled":0,"title":"Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides","issue":"7-8","publication_status":"published","publication":"Biochimica et Biophysica Acta - Bioenergetics","acknowledgement":"This work was supported by the Medical Research Council.","_id":"1968","doi":"10.1016/j.bbabio.2008.03.023","type":"journal_article","page":"711 - 718","publist_id":"5116","date_updated":"2021-01-12T06:54:24Z","volume":1777,"abstract":[{"text":"\n\nComplex I (NADH:ubiquinone oxidoreductase) is the largest protein complex of bacterial and mitochondrial respiratory chains. The first three-dimensional structure of bacterial complex I in vitrified ice was determined by electron cryo-microscopy and single particle analysis. The structure of the Escherichia coli enzyme incubated with either NAD+ (as a reference) or NADH was calculated to 35 and 39 Å resolution, respectively. The X-ray structure of the peripheral arm of Thermus thermophilus complex I was docked into the reference EM structure. The model obtained indicates that Fe-S cluster N2 is close to the membrane domain interface, allowing for effective electron transfer to membrane-embedded quinone. At the current resolution, the structures in the presence of NAD+ or NADH are similar. Additionally, side-view class averages were calculated for the negatively stained bovine enzyme. The structures of bovine complex I in the presence of either NAD+ or NADH also appeared to be similar. These observations indicate that conformational changes upon reduction with NADH, suggested to occur by a range of studies, are smaller than had been thought previously. The model of the entire bacterial complex I could be built from the crystal structures of subcomplexes using the EM envelope described here.","lang":"eng"}],"date_created":"2018-12-11T11:54:58Z","status":"public","author":[{"last_name":"Morgan","first_name":"David","full_name":"Morgan, David J"},{"id":"338D39FE-F248-11E8-B48F-1D18A9856A87","full_name":"Leonid Sazanov","last_name":"Sazanov","orcid":"0000-0002-0977-7989","first_name":"Leonid A"}]}