TY - JOUR
T1 - Supramolecular organizations in the aerobic respiratory chain of Escherichia coli
AU - Carichas Carita, Joao Nuno
N1 - Sousa, Pedro M. F.
Carita, Joao N
PY - 2011/1/1
Y1 - 2011/1/1
N2 - 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 bo(3) 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
AB - 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 bo(3) 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
KW - OXIDATIVE-PHOSPHORYLATION SYSTEM
KW - NADH-UBIQUINONE OXIDOREDUCTASE
KW - BOVINE HEART-MITOCHONDRIA
KW - MITOCHONDRIAL ELECTRON-TRANSPORT
KW - OXIDASE SUPER-COMPLEX
KW - SUCCINATE-DEHYDROGENASE
KW - FORMATE DEHYDROGENASE
KW - THERMOACIDOPHILIC ARCHAEON
KW - TERMINAL OXIDASES
KW - PARACOCCUS-DENITRIFICANS
U2 - 10.1016/j.biochi.2010.10.014
DO - 10.1016/j.biochi.2010.10.014
M3 - Article
VL - 93
SP - 418
EP - 425
JO - Biochimie
JF - Biochimie
SN - 0300-9084
IS - 3
ER -