Department of Biomedical Engineering, Chemistry and Biological Sciences, Stevens Institute of Technology, 1 Castle Point on Hudson, Hoboken, NJ, 07030, USA.
Angew Chem Int Ed Engl. 2016 Nov 21;55(48):15058-15061. doi: 10.1002/anie.201608539. Epub 2016 Oct 31.
HNO plays significant roles in many biological processes. Numerous heme proteins bind HNO, an important step for its biological functions. A systematic computational study was performed to provide the first detailed trends and origins of the effects of iron oxidation state, axial ligand, and protein environment on HNO binding. The results show that HNO binds much weaker with ferric porphyrins than corresponding ferrous systems, offering strong thermodynamic driving force for experimentally observed reductive nitrosylation. The axial ligand was found to influence HNO binding through its trans effect and charge donation effect. The protein environment significantly affects the HNO hydrogen bonding structures and properties. The predicted NMR and vibrational data are in excellent agreement with experiment. This broad range of results shall facilitate studies of HNO binding in many heme proteins, models, and related metalloproteins.
HNO 在许多生物过程中发挥着重要作用。许多血红素蛋白与 HNO 结合，这是其发挥生物功能的重要步骤。本文进行了系统的计算研究，首次详细探讨了铁氧化态、轴向配体和蛋白质环境对 HNO 结合的影响趋势和起源。结果表明，HNO 与三价卟啉铁的结合比相应的二价系统弱得多，为实验观察到的还原亚硝化提供了强大的热力学驱动力。发现轴向配体通过反式效应和电荷供体效应影响 HNO 的结合。蛋白质环境显著影响 HNO 的氢键结构和性质。预测的 NMR 和振动数据与实验结果非常吻合。这些广泛的结果将有助于研究许多血红素蛋白、模型和相关金属蛋白中的 HNO 结合。
