Chemical modification of iron- and manganese-containing superoxide dismutases from Escherichia coli.

Abstract:

:The manganese-containing (MnSOD) and iron-containing (FeSOD) superoxide dismutases from Escherichia coli are extensively (greater than 95%) inactivated by treatment with phenylglyoxal. The relatively high concentrations of phenylglyoxal and high pH required for optimal inactivation suggest that inactivation may be due to modification of an arginine with a "normal" elevated pKa, i.e., one not in an active site cavity where the pKa is likely to be lowered because of lower solvent accessibility and decreased polarity of the local environment. Treatment of either enzyme with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, 2-hydroxy-5-nitrobenzyl bromide, m-chloroperoxybenzoate, or tetranitromethane causes no inactivation, while 2,4,6-trinitrobenzenesulfonate, N-acetylimidazole, or diethyl pyrocarbonate cause 55-75% inactivation of each enzyme. Failure of hydroxylamine to reverse inactivation by the latter two suggests that in each instance loss of activity is due to lysine modification. The previously reported inactivation of FeSOD by H2O2 was further investigated, and no evidence was found for an affinity mechanism, i.e., a reversible binding of peroxide that precedes inactivation.

journal_name

Arch Biochem Biophys

authors

Borders CL Jr,Horton PJ,Beyer WF Jr

doi

10.1016/0003-9861(89)90566-3

subject

Has Abstract

pub_date

1989-01-01 00:00:00

pages

74-80

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(89)90566-3

journal_volume

268

pub_type

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