Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1857, Issue 3, Pages 214-223Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2015.12.004
Keywords
Escherichia coli; Complex I, NADH dehydrogenase; NADH:ubiquinone oxidoreductase; Assembly; Iron-sulfur cluster
Categories
Funding
- Deutsche Forschungsgemeinschaft (DFG) [FOR 929]
- Deutsch-Franzosische Hochschule (DFH) [CDFA 04-07]
- Studienstiftung des deutschen Volkes
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Energy-converting NADH:ubiquinone oxidoreductase, respiratory complex I, couples the electron transfer from NADH to ubiquinone with the translocation of four protons across the membrane. The Escherichia coli complex I is made up of 13 different subunits encoded by the so-called nuo-genes. The electron transfer is catalyzed by nine cofactors, a flavin mononucleotide and eight iron-sulfur (Fe/S)-clusters. The individual subunits and the cofactors have to be assembled together in a coordinated way to guarantee the biogenesis of the active holoenzyme. Only little is known about the assembly of the bacterial complex compared to the mitochondrial one. Due to the presence of so many Fe/S-clusters the assembly of complex I is intimately connected with the systems responsible for the biogenesis of these clusters. In addition, a few other proteins have been reported to be required for an effective assembly of the complex in other bacteria. The proposed role of known bacterial assembly factors is discussed and the information from other bacterial species is used in this review to draw an as complete as possible model of bacterial complex I assembly. In addition, the supramolecular organization of the complex in E. coli is briefly described. This article is part of a Special Issue entitled Organization and dynamics of bioenergetic systems in bacteria, edited by Prof. Conrad Mullineaux. (C) 2015 Elsevier B.V. All rights reserved.
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