The proton pumping stoichiometry of purified mitochondrial complex I reconstituted into proteoliposomes

Alexander Galkin, S. Drose, U. Brandt

Research output: Contribution to journalArticlepeer-review

87 Citations (Scopus)

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. (c) 2006 Elsevier B.V. All rights reserved.
Original languageEnglish
Pages (from-to)1575-1581
Number of pages7
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1757
Issue number12
DOIs
Publication statusPublished - Dec 2006

ASJC Scopus subject areas

  • Biophysics

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