Supramolecular organizations in the aerobic respiratory chain of Escherichia coli

Pedro M.F. Sousa, Sara T.N. Silva, Brian L. Hood, Nuno Charro, João N. Carita, Fátima Vaz, Deborah Penque, Thomas P. Conrads, Ana M.P. Melo

Research output: Contribution to journalArticlepeer-review

42 Scopus citations

Abstract

The organization of respiratory chain complexes in supercomplexes has been shown in the mitochondria of several eukaryotes and in the cell membranes of some bacteria. These supercomplexes are suggested to be important for oxidative phosphorylation efficiency and to prevent the formation of reactive oxygen species. Here we describe, for the first time, the identification of supramolecular organizations in the aerobic respiratory chain of Escherichia coli, including a trimer of succinate dehydrogenase. Furthermore, two heterooligomerizations have been shown: one resulting from the association of the NADH:quinone oxidoreductases NDH-1 and NDH-2, and another composed by the cytochrome bo3 quinol:oxygen reductase, cytochrome bd quinol:oxygen reductase and formate dehydrogenase (fdo). These results are supported by blue native-electrophoresis, mass spectrometry and kinetic data of wild type and mutant E . coli strains.

Original languageEnglish
Pages (from-to)418-425
Number of pages8
JournalBiochimie
Volume93
Issue number3
DOIs
StatePublished - Mar 2011
Externally publishedYes

Keywords

  • Aerobic respiratory chain
  • Bioenergetics
  • Escherichia coli
  • NADH:quinone oxidoreductase
  • Oxygen reductase
  • Supercomplex

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