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Gaining mass: the structure of respiratory complex I - from bacterial towards mitochondria! versions

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CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 33, 期 -, 页码 135-145

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CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2015.08.008

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  1. Medical Research Council [MC_U105674180] Funding Source: Medline
  2. MRC [MC_U105674180] Funding Source: UKRI

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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 angstrom cryo-electron microscopy map of bovine mitochondrial complex I and a similar to 3.8 angstrom 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.

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