We investigated H(+) and Na(+) transport by complex I from Escherichia coli devoid of the NuoL subunit, which is probably part of the ion translocating machinery. We observed that complex I devoid of the NuoL subunit still translocates H(+), although to a smaller extension than the complete version of complex I, but does not transport Na(+). Our results unequivocally reinforce the observation that E. coli complex I transports Na(+) in the opposite direction to that of the H+ and show that NuoL subunit is involved in the translocation of both ions by complex I.
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http://dx.doi.org/10.1016/j.febslet.2014.10.030 | DOI Listing |
Plant Dis
February 2024
Tennessee State University, Otis Floyd Nursery Research Center, 472 Cadillac Lane, McMinnville, Tennessee, United States, 37110;
Plant Dis
December 2023
Anhui Science and Technology University, 177515, Chuzhou, Anhui, China.
Ginger (Zingiber officinale) is an important commercial crop that has been widely cultivated in China for more than 2500 years. One variety, Tongling white ginger, has been grown in the Yi'an District of Tongling city, Anhui province (30°45 N, 117°43 E), China. In August 2022, symptoms of yellowing and wilting were observed on ginger plants, with a disease incidence rate exceeding 20% in the field.
View Article and Find Full Text PDFNature
September 2022
Institute of Science and Technology Austria, Klosterneuburg, Austria.
Complex I is the first enzyme in the respiratory chain, which is responsible for energy production in mitochondria and bacteria. Complex I couples the transfer of two electrons from NADH to quinone and the translocation of four protons across the membrane, but the coupling mechanism remains contentious. Here we present cryo-electron microscopy structures of Escherichia coli complex I (EcCI) in different redox states, including catalytic turnover.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
July 2022
Institute of Biochemistry, Faculty of Chemistry and Pharmacy, Albert-Ludwigs-University, 79104 Freiburg, Germany.
Energy-converting NADH:ubiquinone oxidoreductase, respiratory complex I, is essential for cellular energy metabolism coupling NADH oxidation to proton translocation. The mechanism of proton translocation by complex I is still under debate. Its membrane arm contains an unusual central axis of polar and charged amino acid residues connecting the quinone binding site with the antiporter-type subunits NuoL, NuoM, and NuoN, proposed to catalyze proton translocation.
View Article and Find Full Text PDFMitochondrion
May 2022
Department of Biological Sciences, Southern Methodist University, Dallas, TX 75275-0376, USA. Electronic address:
Respiratory Complex I is the site of a large fraction of the mutations that appear to cause mitochondrial disease. Seven of its subunits are mitochondrially encoded, and therefore, such mutants are particularly difficult to construct in cell-culture model systems. We have selected 13 human clinical mutations found in ND2, ND3, ND4, ND4L, ND5 and ND6 that are generally found at subunit interfaces, and not in critical residues.
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