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.
| Original language | English |
|---|---|
| Pages (from-to) | 135-145 |
| Number of pages | 11 |
| Journal | Current Opinion in Structural Biology |
| Volume | 33 |
| DOIs | |
| Publication status | Published - Aug 2015 |
| Externally published | Yes |
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