INVESTIGADORES
CHALON Miriam Carolina
congresos y reuniones científicas
Título:
Cyanide protects Escherichia coli NADH dehydrogenase activity from
Autor/es:
GALVAN, AE; CHALON M.C.; SCHURIG-BRICCIO L; MINAHK CJ; GENNIS R; BELLOMIO, A
Lugar:
Carlos Paz
Reunión:
Congreso; XLII ReuniĆ³n Anual de la Sociedad Argentina de Biofisica; 2013
Institución organizadora:
Sociedad Argentina de Biofisica
Resumen:
Microcin J25 (MccJ25) is a 21-residue ribosomally synthesized antibacterial lasso peptide. It is produced by Escherichia coli, and is active against close-related bacteria including certain human pathogens like Salmolella enterica and Shigella spp. MccJ25 acts in sensitive bacteria inhibiting the RNA polymerase and the bacterial membrane respiratory chain. The rate of cell oxygen consumption is lower in the presence of the peptide. In a previous report, it was shown that MccJ25 was able to inhibit the NADH dehydrogenase activity in vitro [1]. Interestingly, in the present work we observed that the reaction inhibition decreased to 10% when 6 mM cyanide was added. E. coli has two terminal oxidases, cytochrome bd and cytochrome bo3, which are quinol oxidases. Therefore, the antimicrobial activity and the effect of MccJ25 on NADH dehydrogenase activity from wild type as well as terminal oxidases mutant membranes were assayed. 1- A. Bellomio, P.A.Vincent, B.F. deArcuri, R.N. Farias, R.D.Morero, J. Bacteriol. 189 (2007) 4180?4186.