The energy-converting NADH:ubiquinone oxidoreductase, also known as respiratory complex I, couples the transfer of electrons from NADH to ubiquinone with the translocation of protons across the membrane. Electron microscopy revealed the two-part structure of the complex consisting of a peripheral and a membrane arm. The peripheral arm contains all known cofactors and the NADH-binding site, whereas the membrane arm has to be involved in proton translocation. Owing to this, a conformation-linked mechanism for redox-driven proton translocation is discussed. By means of electron microscopy, we show that both arms of the Escherichia coli complex I are widened after the addition of NADH but not of NADPH. NADH-induced conformational changes were also detected in solution: ATR-FTIR (attenuated total reflection Fourier-transform infrared) of the soluble NADH dehydrogenase fragment of the complex indicates protein re-arrangements induced by the addition of NADH. EPR spectroscopy of surface mutants of the complex containing a covalently bound spin label at distinct positions demonstrates NADH-dependent conformational changes in both arms of the complex.
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October 2008
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September 19 2008
Nucleotide-induced conformational changes in the Escherichia coli NADH:ubiquinone oxidoreductase (complex I)
Thomas Pohl;
Thomas Pohl
*Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, D-79104 Freiburg, Germany
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Daniel Schneider;
Daniel Schneider
*Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, D-79104 Freiburg, Germany
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Ruth Hielscher;
Ruth Hielscher
†Institut de Chimie UMR 7177, Laboratoire de Spectroscopie Vibrationnelle et Electrochimie des Biomolécules, CNRS Université Louis Pasteur, 4 rue Blaise Pascal, F-67070 Strasbourg, France
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Stefan Stolpe;
Stefan Stolpe
*Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, D-79104 Freiburg, Germany
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Katerina Dörner;
Katerina Dörner
*Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, D-79104 Freiburg, Germany
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Markus Kohlstädt;
Markus Kohlstädt
*Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, D-79104 Freiburg, Germany
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Bettina Böttcher;
Bettina Böttcher
‡Structural and Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany
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Petra Hellwig;
Petra Hellwig
†Institut de Chimie UMR 7177, Laboratoire de Spectroscopie Vibrationnelle et Electrochimie des Biomolécules, CNRS Université Louis Pasteur, 4 rue Blaise Pascal, F-67070 Strasbourg, France
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Thorsten Friedrich
Thorsten Friedrich
1
*Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Albertstrasse 21, D-79104 Freiburg, Germany
1To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
March 31 2008
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem Soc Trans (2008) 36 (5): 971–975.
Article history
Received:
March 31 2008
Citation
Thomas Pohl, Daniel Schneider, Ruth Hielscher, Stefan Stolpe, Katerina Dörner, Markus Kohlstädt, Bettina Böttcher, Petra Hellwig, Thorsten Friedrich; Nucleotide-induced conformational changes in the Escherichia coli NADH:ubiquinone oxidoreductase (complex I). Biochem Soc Trans 1 October 2008; 36 (5): 971–975. doi: https://doi.org/10.1042/BST0360971
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