Boucher J L, Genet A, Vadon S, Delaforge M, Mansuy D
Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques URA 400 CNRS, Université René Descartes, Paris, France.
Biochem Biophys Res Commun. 1992 May 15;184(3):1158-64. doi: 10.1016/s0006-291x(05)80004-x.
HRP catalyzes the oxidation of N omega-hydroxy-L-arginine (NOHA) by H2O2 with formation of citrulline and NO2- with initial rates of about 0.7 and 0.2 nmol per nmol HRP per min. In the same manner, cytochromes P450 from rat liver microsomes catalyze the oxidation of NOHA to citrulline and NO2- by cumylhydroperoxide. Inhibitors of these hemeproteins (N3- and CN- for HRP and miconazole for P450) strongly inhibit both citrulline and NO2- formation. Rates of NOHA oxidation by these hemeproteins markedly decrease with time presumably because of their denaturation by nitrogen oxides and of the formation of hemeprotein-iron-NO complexes. These results suggest that NO (and other nitrogen oxides) could be formed from oxidation of NOHA by other enzymes than NO-synthases.
辣根过氧化物酶（HRP）催化H2O2氧化Nω-羟基-L-精氨酸（NOHA），生成瓜氨酸和NO2-，初始速率约为每分钟每纳摩尔HRP 0.7和0.2纳摩尔。同样，大鼠肝微粒体中的细胞色素P450催化NOHA被枯基过氧化氢氧化为瓜氨酸和NO2-。这些血红素蛋白的抑制剂（HRP的N3-和CN-以及P450的咪康唑）强烈抑制瓜氨酸和NO2-的形成。这些血红素蛋白氧化NOHA的速率随时间显著降低，可能是因为它们被氮氧化物变性以及形成了血红素蛋白-铁-NO复合物。这些结果表明，除了一氧化氮合酶外，其他酶也可通过氧化NOHA生成NO（和其他氮氧化物）。
