Navarro F, Villalba J M, Crane F L, Mackellar W C, Navas P
Departamento de Biología Celular, Universidad de Córdoba, Spain.
Biochem Biophys Res Commun. 1995 Jul 6;212(1):138-43. doi: 10.1006/bbrc.1995.1947.
A 34 kDa coenzyme Q reductase has been solubilized and purified from pig liver plasma membranes. The solubilized enzyme reduced coenzyme Q0 with NADH. Ubiquinones with longer isoprenoid side chain such as Q2 and Q10 were also reduced when the quinones and the enzyme were reconstituted into phospholipid liposomes. N-terminal sequencing of an internal peptide showed identity to bovine NADH-cytochrome b5 reductase. Biochemical characterization of the purified enzyme indicated that the coenzyme Q reductase corresponds to an unusual form of NADH-cytochrome b5 reductase.
一种34 kDa的辅酶Q还原酶已从猪肝质膜中溶解并纯化出来。溶解后的酶利用NADH还原辅酶Q0。当将醌类和该酶重新构建到磷脂脂质体中时,具有较长类异戊二烯侧链的泛醌,如Q2和Q10,也会被还原。对一个内部肽段进行N端测序,结果显示其与牛NADH - 细胞色素b5还原酶具有同一性。对纯化酶的生化特性分析表明,该辅酶Q还原酶对应于NADH - 细胞色素b5还原酶的一种特殊形式。