Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide
摘要：
Using highly purified recombinant mitochondrial aconitase, we determined the kinetics and mechanisms of inactivation mediated by nitric oxide (*NO), nitrosoglutathione (GSNO), and peroxynitrite (ONOO(-)). High *NO concentrations are required to inhibit resting aconitase. Brief *NO exposures led to a reversible inhibition competitive with isocitrate (K(I)=35 microM). Subsequently, an...
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DOI：
10.1016/0014-5793(94)80087-1
被引量：
年份：
1994
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