Difference between revisions of "Galkin 2006 Biochim Biophys Acta"
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{{Publication | {{Publication | ||
|title=Galkin A, Dröse S, Brandt U (2006) The proton pumping stoichiometry of purified mitochondrial complex I reconstituted into proteoliposomes. Biochim Biophys Acta 1757:1575-81. | |title=Galkin A, Dröse S, Brandt U (2006) The proton pumping stoichiometry of purified mitochondrial complex I reconstituted into proteoliposomes. Biochim Biophys Acta 1757:1575-81. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17094937 PMID: 17094937] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/17094937 PMID: 17094937 Open Access] | ||
|authors=Galkin A, Droese S, Brandt U | |authors=Galkin A, Droese S, Brandt U | ||
|year=2006 | |year=2006 |
Revision as of 12:38, 20 March 2015
Galkin A, Dröse S, Brandt U (2006) The proton pumping stoichiometry of purified mitochondrial complex I reconstituted into proteoliposomes. Biochim Biophys Acta 1757:1575-81. |
Galkin A, Droese S, Brandt U (2006) Biochim Biophys Acta
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 View the 3.8 H+/2 ē indicated that four protons are pumped per NADH oxidized. For purified Complex I reconstituted into proteoliposomes we measured a very similar pumping stoichiometry of 3.6 H+/2 ē. This is the first demonstration that the proton pump of Complex I stayed fully functional after purification of the enzyme. • Keywords: Complex I, NADH:ubiquinone oxidoreductase, Proton pump, Energy transduction, Mitochondria, Proteoliposome, Yarrowia lipolytica
• O2k-Network Lab: DE Frankfurt Brandt U, DE Frankfurt Droese S
Labels:
Preparation: Isolated mitochondria
Enzyme: Complex I
Coupling state: OXPHOS
HRR: Oxygraph-2k