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J. Biol. Chem., Vol. 268, Issue 30, 22369-22376, Oct, 1993
DH Flint, JF Tuminello and MH Emptage
We report in this paper that highly purified Escherichia coli dihydroxy-
acid dehydratase, fumarase A, fumarase B, and mammalian aconitase are
inactivated by O2- with second order rate constants in the range of 10(6)
to 10(7) M-1 s-1. Each of these enzymes belongs to the hydro- lyase class
and contains catalytically active [4Fe-4S] clusters. Simultaneous with
inactivation by O2- is the release of iron from their clusters. Our working
hypothesis is O2- inactivates these enzymes by oxidizing their clusters to
an unstable oxidation state, and cluster degradation follows. Consistent
with this hypothesis is our observation that spinach dihydroxy-acid
dehydratase, a member of the hydro-lyase class that has a catalytically
active [2Fe-2S] cluster, is not inactivated and does not lose iron in the
presence of O2-. Porcine fumarase, a member of the hydro-lyase class that
does not contain an Fe- S cluster, is also not inactivated by O2-. We also
report the rate constants for the inactivation of E. coli dihydroxy-acid
dehydratase, fumarase A, fumarase B, and mammalian aconitase by O2 are
close to 2 x 10(2) M-1 s-1, and the rate constants for the inactivation of
E. coli dihydroxy-acid dehydratase and mammalian aconitase by H2O2 are
about 10(3) M-1 s-1. E. coli dihydroxy-acid dehydratase has been reported
previously to be inactivated in vivo when cells are grown in hyperbaric O2,
presumably due to the increased O2- generated under these conditions. We
report here that E. coli fumarase A, fumarase B, and aconitase are also
inactivated in vivo by hyperbaric O2. Thermodynamic parameters for the
oxidation of the cluster of aconitase by O2- and O2 are calculated.
The inactivation of Fe-S cluster containing hydro-lyases by superoxide
E. I. du Pont de Nemours and Company, Central Research and Development, Experimental Station, Wilmington, Delaware 19880.
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