@article{1683, abstract = {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.}, author = {Letts, Jame A and Sazanov, Leonid A}, journal = {Current Opinion in Structural Biology}, number = {8}, pages = {135 -- 145}, publisher = {Elsevier}, title = {{Gaining mass: The structure of respiratory complex I-from bacterial towards mitochondrial versions}}, doi = {10.1016/j.sbi.2015.08.008}, volume = {33}, year = {2015}, }