Gaining mass: The structure of respiratory complex I-from bacterial towards mitochondrial versions Letts, Jame A ; https://orcid.org/0000-0002-9864-3586 Sazanov, Leonid A ; https://orcid.org/0000-0002-0977-7989 The 1 MDa, 45-subunit proton-pumping NADH-ubiquinone oxidoreductase (complex I) is the largest complex of the mitochondrial electron transport chain. The molecular mechanism of complex I is central to the metabolism of cells, but has yet to be fully characterized. The last two years have seen steady progress towards this goal with the first atomic-resolution structure of the entire bacterial complex I, a 5 Å cryo-electron microscopy map of bovine mitochondrial complex I and a ∼3.8 Å resolution X-ray crystallographic study of mitochondrial complex I from yeast Yarrowia lipotytica. In this review we will discuss what we have learned from these studies and what remains to be elucidated. Elsevier 2015 info:eu-repo/semantics/article doc-type:article text http://purl.org/coar/resource_type/c_2df8fbb1 https://research-explorer.ista.ac.at/record/1683 Letts JA, Sazanov LA. Gaining mass: The structure of respiratory complex I-from bacterial towards mitochondrial versions. <i>Current Opinion in Structural Biology</i>. 2015;33(8):135-145. doi:<a href="https://doi.org/10.1016/j.sbi.2015.08.008">10.1016/j.sbi.2015.08.008</a> eng info:eu-repo/semantics/altIdentifier/doi/10.1016/j.sbi.2015.08.008 info:eu-repo/semantics/altIdentifier/wos/000365362400016 info:eu-repo/semantics/closedAccess