Redox-Dependent Modulation of Aconitase Activity in Intact Mitochondria

We provide evidence that aconitase is rapidly inactivated and subsequently reactivated when isolated cardiac mitochondria are treated with H2O2

Anne-Laure Bulteau; Masao Ikeda-Saito; Luke I. Szweda

2003

Key concepts

Scholarcy highlights

  • It has previously been reported that exposure of purified mitochondrial or cytoplasmic aconitase to superoxide or hydrogen peroxide leads to release of the Fe-α from the enzyme's2+ cluster and to inactivation
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  • Little is known regarding the response of aconitase to pro-oxidants within intact mitochondria
  • We provide evidence that aconitase is rapidly inactivated and subsequently reactivated when isolated cardiac mitochondria are treated with H2O2
  • These observations suggest that some form of posttranslational modification of aconitase other than release of iron is responsible for enzyme inactivation
  • Depending on the pro-oxidant species, the level and duration of the oxidative stress, and the metabolic state of the mitochondria, aconitase may undergo reversible modulation in activity or progress to2+ cluster disassembly and proteolytic degradation

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