Gaining mass: The structure of respiratory complex I-from bacterial towards mitochondrial versions Review Article


Author(s): Letts, James A.; Sazanov, Leonid A
Title: Gaining mass: The structure of respiratory complex I-from bacterial towards mitochondrial versions
Affiliation IST Austria
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.
Keywords: Thermus thermophilus; proton transport; binding site; cryoelectron microscopy; enzyme binding; enzyme structure; membrane binding; mitochondrial energy transfer; oxidation reduction reaction; protein assembly; taurine cattle; X ray crystallography; Yarrowia lipolytica
Publication Title: Current Opinion in Structural Biology
Volume: 33
ISBN: 0959-440X
Publisher: Elsevier  
Date Published: 2015-08-01
Start Page: 135
End Page: 145
DOI: 10.1016/j.sbi.2015.08.008
Open access: no