Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10871183 | FEBS Letters | 2013 | 6 Pages |
Abstract
The Escherichia coli formate:oxygen oxidoreductase supercomplex (FdOx) was investigated with respect to function and composition. Formate oxidoreductase activity was detected in blue native polyacrylamide gel electrophoresis (BN-PAGE) resolved membranes of E. coli, which were also capable of cyanide sensitive formate:oxygen oxidoreductase activity. The latter was compromised in strains devoid of specific oxygen reductases, particularly, in those devoid of cytochrome bo3 or bdI. A principal component analysis (PCA) integrating E. coli aerobic respiratory chain gene transcription, enzyme activity and growth dynamics was performed, correlating formate:oxygen oxidoreductase activity and the transcription of the genes encoding cytochromes bo3 and bdI, and corroborating previous evidence that associated these complexes in FdOx.
Keywords
BN-PAGEndh-2FDoxOxygen reductaseDeamino-NADHK3[Fe(CN)6]NDH-1dichlorophenol indophenolMOPSVmaxNBTDDMDCPIPPMSFDH3-(N-morpholino) propanesulfonic aciddodecyl-β-D-maltosideNADH:quinone oxidoreductasePCAnitroblue tetrazoliumEscherichia coliblue native polyacrylamide gel electrophoresisOxidoreductaseBacteriaPrincipal component analysisGene transcriptionmaximal velocityFormate dehydrogenasePotassium ferricyanidephenazine methosulfatearbitrary units
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Authors
Pedro M.F. Sousa, Marco A.M. Videira, Ana M.P. Melo,