These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Asp563 of the horizontal helix of subunit NuoL is involved in proton translocation by the respiratory complex I. Author: Steimle S, Willistein M, Hegger P, Janoschke M, Erhardt H, Friedrich T. Journal: FEBS Lett; 2012 Mar 23; 586(6):699-704. PubMed ID: 22326235. 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.[Abstract] [Full Text] [Related] [New Search]