Department of Chemistry, The Pennsylvania State University, University Park, 332 Chemistry Building, Pennsylvania, PA 16802, USA.
Photosynth Res. 2009 Nov-Dec;102(2-3):295-304. doi: 10.1007/s11120-009-9406-6.
(57)Fe-Mössbauer spectroscopy is a method that probes transitions between the nuclear ground state (I=1/2) and the first nuclear excited state (I=3/2). This technique provides detailed information about the chemical environment and electronic structure of iron. Therefore, it has played an important role in studies of the numerous iron-containing proteins and enzymes. In conjunction with the freeze-quench method, (57)Fe-Mössbauer spectroscopy allows for monitoring changes of the iron site(s) during a biochemical reaction. This approach is particularly powerful for detection and characterization of reactive intermediates. Comparison of experimentally determined Mössbauer parameters to those predicted by density functional theory for hypothetical model structures can then provide detailed insight into the structures of reactive intermediates. We have recently used this methodology to study the reactions of various mononuclear non-heme-iron enzymes by trapping and characterizing several Fe(IV)-oxo reaction intermediates. In this article, we summarize these findings and demonstrate the potential of the method.
(57)Fe-穆斯堡尔谱学是一种探测原子核基态（I=1/2）和第一激发核态（I=3/2）之间跃迁的方法。该技术提供了有关铁的化学环境和电子结构的详细信息。因此，它在研究众多含铁的蛋白质和酶方面发挥了重要作用。结合冷冻淬火法，(57)Fe-穆斯堡尔谱学可用于在生化反应过程中监测铁位的变化。这种方法对于检测和表征反应中间体特别有效。然后，将实验测定的穆斯堡尔参数与假设模型结构的密度泛函理论预测的参数进行比较，可以深入了解反应中间体的结构。我们最近使用该方法通过捕获和表征几种 Fe(IV)-氧反应中间体来研究各种单核非血红素铁酶的反应。在本文中，我们总结了这些发现并展示了该方法的潜力。
