A proposed reaction mechanism for rice NADPH thioredoxin reductase C, an enzyme with protein disulfide reductase activity
A proposed reaction mechanism for rice NADPH thioredoxin reductase C, an enzyme with protein disulfide reductase activity
复制标题
DOI：
10.1016/j.febslet.2009.03.067
复制
发表时间：
2009-05-06
期刊：
影响因子：
3.5
通讯作者：
Javier Cejudo, Francisco
中科院分区：
文献类型：
--
作者：
Manuel Perez-Ruiz, Juan;Javier Cejudo, Francisco
NADPH硫氧还蛋白还原酶C（NTRC）是一种有趣的NTR，在C-末端具有硫氧还蛋白（Trx）结构域，能够缀合2-Cys过氧化物氧还蛋白（Prx）还原的两种活性。NTRC在NADPH存在下是二聚体，并通过NTRC的Cys 377和2-Cys Prx的Cys 61之间的混合二硫化物通过Trx模块与二聚体2-Cys Prx相互作用。NTR和Trx活性位点的NTRC变体是无活性的，但两种变体的1：1混合物允许部分恢复活性，表明在催化过程中电子的亚基间转移。基于这些结果，我们提出了一个模型的反应机理NTRC。
NADPH thioredoxin reductase C ( NTRC) is an interesting NTR with a thioredoxin (Trx) domain at the C-terminus, able to conjugate both activities for 2-Cys peroxiredoxin (Prx) reduction. NTRC is dimeric in the presence of NADPH and interacted with dimeric 2-Cys Prx through the Trx module by a mixed disulfide between Cys377 of NTRC and Cys61 of the 2-Cys Prx. NTRC variants of both NTR and Trx active sites were inactive, but 1: 1 mixtures of both variants allowed partial recovery of activity suggesting inter-subunit transfer of electrons during catalysis. Based on these results we propose a model for the reaction mechanism of NTRC.