@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},
}