Multiple-timescale photoreactivity of a model compound related to the active site of [FeFe]-hydrogenase.
Multiple-timescale photoreactivity of a model compound related to the active site of [FeFe]-hydrogenase.
复制标题
与 [FeFe]-氢化酶活性位点相关的模型化合物的多时间尺度光反应性。
DOI：
10.1021/ic800568k
复制
发表时间：
2008
影响因子：
4.6
通讯作者：
Ridley AR
中科院分区：
文献类型：
--
作者：
Ridley AR
研究了铁氢化酶系统的模型化合物（μ-S(CH2)3S）Fe2(CO)6(1)的紫外光解反应。采用超快紫外泵浦红外（IR）探针光谱、稳态傅立叶变换红外光谱方法和密度泛函理论模拟，确定了1在350 nm的烷烃溶液中辐照可在50 ps内形成16电子配合物（μ-S(CH2)3S）Fe2(CO)5的两个同分异构体，并有弱结合溶剂加合物的证据。随后在几分钟的时间尺度上恢复。这些研究是首次尝试研究这些酶活性位点模型在羰基配体光解后在溶液中的光化学和反应性。
Ultraviolet (UV) photolysis of (μ-S(CH2)3S)Fe2(CO)6(1), a model compound of the Fe-hydrogenase enzyme system, has been carried out. When ultrafast UV-pump infrared (IR)-probe spectroscopy, steady-state Fourier transform IR spectroscopic methods, and density functional theory simulations are employed, it has been determined that irradiation of1in an alkane solution at 350 nm leads to the formation of two isomers of the 16-electron complex (μ-S(CH2)3S)Fe2(CO)5within 50 ps with evidence of a weakly associated solvent adduct complex.1is subsequently recovered on timescales covering several minutes. These studies constitute the first attempt to study the photochemistry and reactivity of these enzyme active site models in solution following carbonyl ligand photolysis.