作者: Yisong GUO , Hongxin WANG , Yuming XIAO , Matt C SMITH , Xiaowei ZHANG
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摘要: Iron-Sulfur (Fe-S) proteins are among the most common and ancient enzymes and electron-transfer agents in nature. They play key roles in photosynthesis, respiration, and the metabolism of small molecules, such as H2, CO and N2. Fe-S proteins contain Fe-S clusters as active centers of the proteins, where chemical reactions happen. Conventional Mössbauer spectroscopy has achieved a great success to determine electronic structures of Fe-S clusters in Fe-S proteins [1]. Nuclear forward scattering (NFS) has been used to study minerals in earth’s mantle, also it has been used to study model compounds in heme proteins [2]. Compared with conventional Mössbauer spectroscopy, instead of using radioactive sources, NFS uses synchrotron radiation to excite nuclei and monitor the decay of nuclear excited state in time domain; quantum beat pattern can be observed if the nuclear states contain nuclear hyperfine …