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The reactions of the NAD radical (NAD.) with ferric horseradish peroxidase and with compounds I and II were investigated by pulse radiolysis. NAD. reacted with the ferric enzyme and with compound I to form the ferrous enzyme and compound II with second-order rate constants of 8 X 10(8) and 1.5 X 10(8) M-1 s-1, respectively, at pH 7.0. In contrast, no reaction of NAD. with native compound II at pH 10.0 nor with diacetyldeutero-compound II at pH 5.0-8.0 could be detected. Other reducing species generated by pulse radiolysis, such as hydrated electron (eaq-), superoxide anion (O2-), and benzoate anion radical, could not reduce compound II of the enzyme to the ferric state, although the methylviologen radical reduced it. The results are discussed in relation to the mechanism of catalysis of the one-electron oxidation of substrates by peroxidase.
K Kobayashi, and
K Hayashi, and
A J Swallow
March 1985,
The Biochemical journal,
K Kobayashi, and
K Hayashi, and
A J Swallow
July 2006,
Journal of the American Chemical Society,
K Kobayashi, and
K Hayashi, and
A J Swallow
April 1968,
Biochemical and biophysical research communications,
K Kobayashi, and
K Hayashi, and
A J Swallow
December 1982,
Biochemical and biophysical research communications,
K Kobayashi, and
K Hayashi, and
A J Swallow
April 1957,
The Journal of biological chemistry,
K Kobayashi, and
K Hayashi, and
A J Swallow
February 1972,
Journal of biochemistry,
K Kobayashi, and
K Hayashi, and
A J Swallow
December 1974,
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K Kobayashi, and
K Hayashi, and
A J Swallow
January 1994,
Biochimica et biophysica acta,
K Kobayashi, and
K Hayashi, and
A J Swallow
March 1988,
Toxicology and applied pharmacology,
K Kobayashi, and
K Hayashi, and
A J Swallow
January 1992,
Chemical research in toxicology,
