Difference between revisions of "Letts 2015 Curr Opin Struct Biol"
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|title=Letts JA, Sazanov LA (2015) Gaining mass: the structure of respiratory complex I-from bacterial towards mitochondrial versions. Curr Opin Struct Biol 33:135-45. doi | |title=Letts JA, Sazanov LA (2015) Gaining mass: the structure of respiratory complex I-from bacterial towards mitochondrial versions. Curr Opin Struct Biol 33:135-45. https://doi.org/10.1016/j.sbi.2015.08.008 | ||
|info=[https://pubmed.ncbi.nlm.nih.gov/26387075/ PMID: 26387075] | |info=[https://pubmed.ncbi.nlm.nih.gov/26387075/ PMID: 26387075] | ||
|authors=Letts JA, Sazanov Leonid A | |authors=Letts JA, Sazanov Leonid A | ||
Latest revision as of 20:07, 6 November 2023
| Letts JA, Sazanov LA (2015) Gaining mass: the structure of respiratory complex I-from bacterial towards mitochondrial versions. Curr Opin Struct Biol 33:135-45. https://doi.org/10.1016/j.sbi.2015.08.008 |
Letts JA, Sazanov Leonid A (2015) Curr Opin Struct Biol
Abstract: The 1MDa, 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.
• Bioblast editor: Gnaiger E
Labels:
Organism: Bovines, Eubacteria
Enzyme: Complex I
