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A giant molecular proton pump: structure and mechanism of respiratory complex I

Journal

NATURE REVIEWS MOLECULAR CELL BIOLOGY
Volume 16, Issue 6, Pages 375-388

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nrm3997

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Funding

  1. Royal Society
  2. European Molecular Biology Organization (EMBO)
  3. UK Medical Research Council
  4. MRC [MC_U105674180] Funding Source: UKRI
  5. Medical Research Council [MC_U105674180] Funding Source: researchfish

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The mitochondrial respiratory chain, also known as the electron transport chain (ETC), is crucial to life, and energy production in the form of ATP is the main mitochondrial function. Three proton-translocating enzymes of the ETC, namely complexes I, III and IV, generate proton motive force, which in turn drives ATP synthase (complex V). The atomic structures and basic mechanisms of most respiratory complexes have previously been established, with the exception of complex I, the largest complex in the ETC. Recently, the crystal structure of the entire complex I was solved using a bacterial enzyme. The structure provided novel insights into the core architecture of the complex, the electron transfer and proton translocation pathways, as well as the mechanism that couples these two processes.

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