苯并(a)芘与过氧化物酶的结合及其被过氧化物酶 - H2O2 中间体氧化。
Binding of benzo(a)pyrene with peroxidase and its oxidation by peroxidase-H2O2 intermediate.
作者信息
Akagawa S, Momoi H, Yagi M
出版信息
Cancer Biochem Biophys. 1984 Sep;7(3):213-29.
The oxidation of benzo(a)pyrene (BP) by horseradish peroxidase (HRP) (EC 1.11.1.7) was examined spectrophotometrically by the decomposition of peroxidase-H2O2 intermediate "compound II." The rate constant of the oxidation of BP was 9.5 X 10(4) M-1 sec-1. The oxidation of BP by HRP was inhibited at high BP concentrations, and the hydrogen donor (BP) inhibition constant, KA', was 1.48 microM. The association constant, Kassoc, of the formation of a complex of BP and HRP at 403 nm was 4.37 X 10(4) M-1. The oxidation products of BP have been identified as 1,6-, 3,6- and 6,12-quinone BP. These products showed no mutagenicity in the mutagenicity assay.
通过辣根过氧化物酶（HRP，EC 1.11.1.7）催化的过氧化物酶-H₂O₂中间体“化合物II”的分解，用分光光度法研究了苯并(a)芘（BP）的氧化。BP氧化的速率常数为9.5×10⁴ M⁻¹ s⁻¹。在高BP浓度下，HRP对BP的氧化受到抑制，氢供体（BP）抑制常数KA'为1.48 μM。在403 nm处，BP与HRP形成复合物的缔合常数Kassoc为4.37×10⁴ M⁻¹。BP的氧化产物已鉴定为1,6-、3,6-和6,12-醌BP。这些产物在致突变性试验中未显示出致突变性。
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