Department of Chemistry, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-0802, Japan.
Department of Medical Life Science, Graduate School of Medical Life Science, Yokohama City University, Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.
Faraday Discuss. 2022 May 18;234(0):304-314. doi: 10.1039/d1fd00065a.
CYP152A1 (cytochrome P450) is a fatty acid peroxygenase, which specifically catalyses the oxidation of long-chain fatty acids using hydrogen peroxide as an oxidant. We have found that CYP152A1 possesses catalase activity, which competes with the hydroxylation of long-chain fatty acids, the oxidation of non-native substrates, and haem degradation. Using hydrogen peroxide, Compound I of CYP152A1 could not be observed, due to its swift decomposition catalase activity, where Compound I reacts with another molecule of hydrogen peroxide to form O. In contrast, a clear spectral change indicative of Compound I formation was observed when CPBA was employed as the oxidant. This work presents valuable insights into an important role for the catalase activity of CYP152A1 in avoiding enzyme deactivation when no substrate is available for oxidation.
CYP152A1（细胞色素 P450）是一种脂肪酸过氧化物酶，它特异性地使用过氧化氢作为氧化剂来催化长链脂肪酸的氧化。我们发现 CYP152A1 具有过氧化氢酶活性，该活性与长链脂肪酸的羟化、非天然底物的氧化和血红素降解竞争。由于其迅速分解为过氧化氢酶活性，因此不能观察到 CYP152A1 的复合物 I 用过氧化氢，其中复合物 I 与另一个分子的过氧化氢反应形成 O。相比之下，当使用 CPBA 作为氧化剂时，观察到明显的光谱变化，表明复合物 I 的形成。这项工作为 CYP152A1 的过氧化氢酶活性在没有底物可用于氧化时避免酶失活提供了有价值的见解。
