Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis.
Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis.
复制标题
来自热液海热菌的十二聚多铜氧化酶的晶体结构。
DOI：
10.1107/s205979832100944x
复制
发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Georgiadis,MillieM
中科院分区：
文献类型：
--
作者：
Paavola,JosephL;Battistin,Umberto;Ogata,CraigM;Georgiadis,MillieM
Multicopper oxidases (MCOs) represent a diverse family of enzymes that catalyze the oxidation of either an organic or a metal substrate with concomitant reduction of dioxygen to water. These enzymes contain variable numbers of cupredoxin domains, two, three or six per subunit, and rely on four copper ions, a single type I copper and three additional copper ions organized in a trinuclear cluster (TNC), with one type II and two type III copper ions, to catalyze the reaction. Here, two crystal structures and the enzymatic characterization of Marinithermus hydrothermalis MCO, a two-domain enzyme, are reported. This enzyme decolorizes Congo Red dye at 70°C in the presence of high halide concentrations and may therefore be useful in the detoxification of industrial waste that contains dyes. In two distinct crystal structures, MhMCO forms the trimers seen in other two-domain MCOs, but differs from these enzymes in that four trimers interact to create a dodecamer. This dodecamer of MhMCO forms a closed ball-like structure and has implications for the sequestration of bound divalent metal ions as well as substrate accessibility. In each subunit of the dodecameric structures, a Trp residue, Trp351, located between the type I and TNC sites exists in two distinct conformations, consistent with a potential role in facilitating electron transfer in the enzyme.
