The atomistic details of electron tunneling along seven Fe/S clusters in complex I, a key enzyme in cellular respiration, are examined by using the tunneling current theory and computer simulations. Distinct electron tunneling pathways are identified with several key residues which are further characterized by sensitivity of electron transfer rates to their mutations, examined in simulations and their conservation among complex I homologues. Internal water between protein subunits is identified as an essential mediator enhancing the overall electron transfer rate. 

Electron tunneling in respiratory complex I

243rd National Meeting (2012)

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