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FEBS Lett. 2012 Mar 23;586(6):699-704. doi: 10.1016/j.febslet.2012.01.056. Epub 2012 Feb 3.

Asp563 of the horizontal helix of subunit NuoL is involved in proton translocation by the respiratory complex I.

Author information

1
Albert-Ludwigs-Universität Freiburg, Institut für Organische Chemie und Biochemie, Freiburg i. Br., Germany.

Abstract

The NADH:ubiquinone oxidoreductase couples the electron transfer from NADH to ubiquinone with the translocation of protons across the membrane. It contains a 110Å long helix running parallel to the membrane part of the complex. Deletion of the helix resulted in a reduced H(+)/e(-) stoichiometry indicating its direct involvement in proton translocation. Here, we show that the mutation of the conserved amino acid D563(L), which is part of the horizontal helix of the Escherichia coli complex I, leads to a reduced H(+)/e(-) stoichiometry. It is discussed that this residue is involved in transferring protons to the membranous proton translocation site.

PMID:
22326235
DOI:
10.1016/j.febslet.2012.01.056
[Indexed for MEDLINE]
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