CEITEC-Central European Institute of Technology, Masaryk University, Kamenice 5/A4, 62500, Brno, Czech Republic.
Department of Condensed Matter Physics, Faculty of Science, Masaryk University, Kotlářská 2, 61137, Brno, Czech Republic.
Chemistry. 2017 Mar 8;23(14):3246-3250. doi: 10.1002/chem.201605307. Epub 2017 Feb 8.
Anion-π interactions have been shown to stabilize flavoproteins and to regulate the redox potential of the flavin cofactor. They are commonly attributed to electrostatic forces. Herein we show that anion-flavin interactions can have a substantial charge-transfer component. Our conclusion emanates from a multi-approach theoretical analysis and is backed by previously reported observations of absorption bands, originating from charge transfer between oxidized flavin and proximate cysteine thiolate groups. This partial covalency of anion-flavin contacts renders classical simulations of flavoproteins questionable.
阴离子-π 相互作用已被证明可以稳定黄素蛋白并调节黄素辅因子的氧化还原电位。它们通常归因于静电力。在此，我们表明阴离子-黄素相互作用可以具有很大的电荷转移分量。我们的结论源自多方法理论分析，并得到了先前报道的吸收带观察结果的支持，这些吸收带源自氧化黄素和邻近半胱氨酸硫醇基团之间的电荷转移。这种阴离子-黄素接触的部分共价性使得对黄素蛋白的经典模拟受到质疑。
