Details

Autor(en) / Beteiligte

• Kuo, C.F.
• Mashino, T.
• Fridovich, I.

Titel

alpha, beta-Dihydroxyisovalerate dehydratase. A superoxide-sensitive enzyme

Ist Teil von

• The Journal of biological chemistry, 1987-04, Vol.262 (10), p.4724-4727

Ort / Verlag

Bethesda, MD: Elsevier Inc

Erscheinungsjahr

1987

Quelle

Elektronische Zeitschriftenbibliothek - Freely accessible e-journals

Beschreibungen/Notizen

• Increasing the intracellular flux of O-2 by incubating aerobic Escherichia coli with paraquat or plumbagin markedly lowered the alpha, beta-dihydroxyisovalerate dehydratase activity detectable in extracts from these cells. This effect was not seen in the absence of dioxygen and was exacerbated by inhibiting protein biosynthesis with chloramphenicol. These effects of paraquat and of plumbagin were both time- and concentration-dependent. Transfer of E. coli from aerobic to anaerobic conditions caused a rebound of the dehydratase activity, in the continued presence of paraquat and of chloramphenicol, indicating the presence of a mechanism for reactivating this enzyme. The instability of the dehydratase activity in cell extracts was exacerbated by selective removal of superoxide dismutase, but not of catalase, by immunoprecipitation. Addition of exogenous superoxide dismutase reversed the effect of immunoprecipitation; whereas catalase or inactive superoxide dismutase were ineffective. We conclude that the dehydratase is inactivated by O-2. This could account for the bacteriostatic effects of dioxygen and of paraquat.