Department of Biochemistry, University of Illinois, Urbana, IL 61801, USA.
Angew Chem Int Ed Engl. 2013 May 10;52(20):5342-5. doi: 10.1002/anie.201300760. Epub 2013 Apr 10.
Raman spectra of oxygenated intermediates of Nanodisc incorporated human CYP17 in the presence of natural substrates directly confirm that substrate structure effectively alters H-bonding interactions with the critical Fe-O-O fragment so as to dictate its predisposition for one of two alternative reaction pathways, providing a realistic structural explanation for substrate control of CYP17 reactivity that has profound physiological implications.
纳米盘包裹的人源 CYP17 与天然底物存在时的含氧中间产物的拉曼光谱直接证实,底物结构有效地改变了与关键 Fe-O-O 片段的氢键相互作用,从而决定了其倾向于两种替代反应途径中的一种,为 CYP17 反应性的底物控制提供了现实的结构解释,这具有深远的生理意义。