Department of Botany, Aligarh Muslim University, Aligarh, Uttar Pradesh, 202002, India.
Department of Environmental Science, School of Earth and Environmental Sciences, Central University of Himachal Pradesh, Shahpur, District-Kangra, Himachal Pradesh, 176206, India.
Int J Biochem Cell Biol. 2018 Oct;103:74-80. doi: 10.1016/j.biocel.2018.08.007. Epub 2018 Aug 18.
Cytochrome P are involved in a variety of monooxygenation reactions that require electron transfer from one redox partner to the other. We have recently shown the catalytic mechanism of a cytochrome P monooxygenase like protein (encoded by tri11 gene) that catalyzes the hydroxylation of 12,13-epoxytrichothec-9-ene (EPT) to produce trichodermol in the trichothecene biosynthetic pathway of trichodermin and harzianum A in Trichoderma brevicompactum [J Biol Inorg Chem. 22(8):1197-1209. doi: https://doi.org/10.1007/s00775-017-1496-6]. In the present work we have analyzed the effects of interaction of CPR FMN domain, a redox partner of tri11 protein, on its catalysis. The analysis of protein-protein complex interface showed various important contacts between the two protein partners that may aid in the process of electron transfer. The redox partner binding with tri11 protein on proximal side elicited catalytically important changes on the oppositely situated distal side that may help in stabilizing the active site and may play positive roles during the catalysis.
细胞色素 P 参与多种单加氧反应，需要电子从一个氧化还原伴侣转移到另一个。我们最近研究了一种细胞色素 P 单加氧酶样蛋白（由 tri11 基因编码）的催化机制，该蛋白催化 12,13-环氧三噻烷（EPT）的羟化，以在 Trichoderma brevicompactum 的 Trichodermin 和 harzianum A 的三噻烷生物合成途径中产生 Trichodermol [J Biol Inorg Chem. 22(8):1197-1209. doi: https://doi.org/10.1007/s00775-017-1496-6]。在本工作中，我们分析了 CPR FMN 结构域（tri11 蛋白的氧化还原伴侣）相互作用对其催化作用的影响。对蛋白质-蛋白质复合物界面的分析表明，两个蛋白质伴侣之间存在各种重要的接触，这可能有助于电子转移过程。氧化还原伴侣与 tri11 蛋白在近端结合，在相对的远端引起催化重要的变化，这可能有助于稳定活性位点，并在催化过程中发挥积极作用。
