[{"date_published":"2008-07-01T00:00:00Z","citation":{"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.","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.","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","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.","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.","short":"D. Morgan, L.A. Sazanov, Biochimica et Biophysica Acta - Bioenergetics 1777 (2008) 711–718."},"publication":"Biochimica et Biophysica Acta - Bioenergetics","page":"711 - 718","quality_controlled":0,"uri_base":"https://research-explorer.ista.ac.at","day":"01","month":"07","dc":{"creator":["Morgan, David J","Leonid Sazanov"],"description":["\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."],"type":["info:eu-repo/semantics/article","doc-type:article","text","http://purl.org/coar/resource_type/c_6501"],"identifier":["https://research-explorer.ista.ac.at/record/1968"],"date":["2008"],"relation":["info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbabio.2008.03.023"],"publisher":["Elsevier"],"title":["Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides"],"rights":["info:eu-repo/semantics/closedAccess"],"source":["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"]},"author":[{"last_name":"Morgan","first_name":"David"},{"last_name":"Sazanov","first_name":"Leonid A","orcid":"0000-0002-0977-7989","id":"338D39FE-F248-11E8-B48F-1D18A9856A87"}],"volume":1777,"date_updated":"2021-01-12T06:54:24Z","dini_type":"doc-type:article","date_created":"2018-12-11T11:54:58Z","acknowledgement":"This work was supported by the Medical Research Council.","_id":"1968","intvolume":" 1777","publication_status":"published","status":"public","issue":"7-8","publist_id":"5116","abstract":[{"lang":"eng"}],"extern":1,"type":"journal_article"}]