X-ray absorption spectroscopic analysis of metal-containing proteins and peptides
Shokes, Jacob Estes
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X-ray absorption spectroscopy (XAS) was used to characterize the binding sites of numerous transition metals in different proteins and peptides providing detailed structural and/or functional information about the system. In particular, it resulted in direct structural evidence of an Fe-Se interaction in heterodisulfide reductase reacted with CoM-SeH, further validating the proposed mechanism of Duin and colleagues involving the direct attachment of CoM-SH to an 3+iron, thus forming a [4Fe-4S] cluster with a five-coordinate Fe site. Studies on metals in fibril formation presented vital structural details of Zn(II) and Cu(II) complexes along the self-assembly pathway, which is crucial for understanding and possible prevention of amyloid formation at the early stage of Alzheimer’s disease. Additionally, studies on heavy metal responsive regulator proteins have provided a framework for understanding metal selectivity helping to bridge the gap between inorganic and biological chemistry that can be applied to the understanding of nature’s selection process. Other biological systems that were studied include purine hydroxylase, heavy metal resistance proteins, and iron-sulfur cluster proteins.