The proton pumping stoichiometry of purified mitochondrial complex I reconstituted into proteoliposomes. Academic Article uri icon

Overview

abstract

  • NADH:ubiquinone oxidoreductase (complex I) is the largest and most complicated enzyme of aerobic electron transfer. The mechanism how it uses redox energy to pump protons across the bioenergetic membrane is still not understood. Here we determined the pumping stoichiometry of mitochondrial complex I from the strictly aerobic yeast Yarrowia lipolytica. With intact mitochondria, the measured value of 3.8H(+)/2e indicated that four protons are pumped per NADH oxidized. For purified complex I reconstituted into proteoliposomes we measured a very similar pumping stoichiometry of 3.6H(+)/2e . This is the first demonstration that the proton pump of complex I stayed fully functional after purification of the enzyme.

publication date

  • October 7, 2006

Research

keywords

  • Electron Transport Complex I
  • Mitochondria
  • Proton Pumps

Identity

Scopus Document Identifier

  • 33751556659

Digital Object Identifier (DOI)

  • 10.1016/j.bbabio.2006.10.001

PubMed ID

  • 17094937

Additional Document Info

volume

  • 1757

issue

  • 12