ABSTRACT Photoactive proteins that efficiently and selectively transfer light energy into a physical response are ubiquitous in nature. The small molecule chromophores that lie at the heart of these processes often exist as closed-shell anions following deprotonation in proton-transfer reactions. This review highlights the important role that anion photoelectron spectroscopy, combined with computational chemistry calculations, is playing in improving our understanding of the electronic structure and relaxation dynamics of these protein chromophores. We discuss key aspects of anion photoelectron spectroscopy. We then review recent anion photoelectron spectroscopy studies of the deprotonated chromophore anions found in green fluorescent protein (GFP), photoactive yellow protein (PYP) and the deprotonated luciferin anion found in the luciferase enzyme.

中文翻译：

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蛋白质发色团的阴离子光电子能谱

摘要 光活性蛋白在自然界中普遍存在，能有效地、选择性地将光能转化为物理反应。位于这些过程核心的小分子发色团通常在质子转移反应中去质子化后以闭壳阴离子的形式存在。这篇综述强调了阴离子光电子能谱结合计算化学计算在提高我们对这些蛋白质发色团的电子结构和弛豫动力学的理解方面发挥的重要作用。我们讨论阴离子光电子能谱的关键方面。然后，我们回顾了最近在绿色荧光蛋白 (GFP) 中发现的去质子化发色团阴离子的阴离子光电子能谱研究，