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Trends Cell Biol. 2018 Oct;28(10):835-867. doi: 10.1016/j.tcb.2018.06.006. Epub 2018 Jul 26.

Mammalian Mitochondrial Complex I Structure and Disease-Causing Mutations.

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Institute of Science and Technology Austria, Am Campus 1, Klosterneuburg 3400, Austria; Present address: The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.
Institute of Science and Technology Austria, Am Campus 1, Klosterneuburg 3400, Austria. Electronic address:


Complex I has an essential role in ATP production by coupling electron transfer from NADH to quinone with translocation of protons across the inner mitochondrial membrane. Isolated complex I deficiency is a frequent cause of mitochondrial inherited diseases. Complex I has also been implicated in cancer, ageing, and neurodegenerative conditions. Until recently, the understanding of complex I deficiency on the molecular level was limited due to the lack of high-resolution structures of the enzyme. However, due to developments in single particle cryo-electron microscopy (cryo-EM), recent studies have reported nearly atomic resolution maps and models of mitochondrial complex I. These structures significantly add to our understanding of complex I mechanism and assembly. The disease-causing mutations are discussed here in their structural context.


NADH–ubiquinone oxidoreductase; cryo-electron microscopy; mitochondrial disease; mitochondrial respiratory chain; respiratory complex I

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