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J. Biol. Chem., Vol. 269, Issue 4, 2405-2410, Jan, 1994
K Uchida and S Kawakishi
Inactivation of Cu,Zn-superoxide dismutase (Cu,Zn-SOD) by its own reaction
product H2O2 is a well-known phenomenon. Generation of the hydroxyl radical
has been a matter of great concern, and the target molecule has been
regarded as its own active site histidine residues, whose oxidized forms
have not yet been identified (Hodgson, E.K., and Fridovich, I. (1975)
Biochemistry 14, 5294-5299). Here we report on the identification of
oxidized histidines generated at the active site of Cu,Zn-SOD by reaction
with H2O2. When bovine erythrocyte Cu,Zn-SOD (0.5 mg/ml) was treated with 5
mM H2O2 in 50 mM sodium phosphate buffer (pH 7.2), histidine was
significantly lost; however, except for a significant increase in aspartate
and glutamate, nothing new appeared in the amino acid analysis of oxidized
Cu,Zn-SOD. On the other hand, the hydrolysates of oxidized Cu,Zn-SOD
involved an unknown product that was detectable by reverse-phase high
performance liquid chromatography with electrochemical detection. The
product was found to be identical to 2-oxo-histidine that had been
discovered as the major oxidation product of histidine and its peptides
treated with a copper/ascorbate- free radical generating system. The main
product present in the hydrolysate of H2O2-treated Cu,Zn-SOD was
2-oxo-histidine. Approximately 0.66 mol/mol subunit was formed when
Cu,Zn-SOD was treated with 5 mM H2O2 for 30 min. Both metal chelators and
the hydroxyl radical scavengers only slightly inhibited the 2-oxo-histidine
formation (10-39%), suggesting that the active species were produced mainly
inside the ligands of the Cu2+ in the enzyme. Trypsin digestion of
H2O2-treated Cu,Zn-SOD showed selective reactions at the sequences of
Gly24-Lys67 and Thr114-Arg126, in that histidine residues locate at the
active center. Two new products derived from those peptides appeared in the
tryptic map. Amino acid analysis of both products demonstrated the loss of
only histidine. One of them derived from Thr114-Arg126 contained an
equimolar amount of 2-oxo-histidine, indicating that His-118 was converted
selectively to 2-oxo-histidine; however, another product derived from
Gly24-Lys67 contained only 0.085 mol of 2-oxo-histidine/mol of peptide,
suggesting that the product is a mixture consisting of unidentified forms
of oxidized histidine. Taken together, the present study provided direct
evidence that 2-oxo- histidine was generated in the Cu,Zn-SOD exposed to
H2O2 and that its generation was selective at histidine 118 of the active
site of the enzyme.
Identification of oxidized histidine generated at the active site of Cu,Zn-superoxide dismutase exposed to H2O2. Selective generation of 2- oxo-histidine at the histidine 118
Laboratory of Food and Biodynamics, Nagoya University School of Agriculture, Japan.
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