Molybdenum Site Structure of MOSC Family Proteins

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• 作者：Logan J. Giles ; Christian Ruppelt ; Jing Yang ; Ralf R. Mendel ; Florian Bittner ; Martin L. Kirk
• 刊名：Inorganic Chemistry
• 出版年：2014
• 出版时间：September 15, 2014
• 年：2014
• 卷：53
• 期：18
• 页码：9460-9462
• 全文大小：243K
• ISSN：1520-510X

文摘

Mo K-edge X-ray absorption spectroscopy has been used to probe as-isolated structures of the MOSC family proteins pmARC-1 and HMCS-CT. The Mo K-edge near-edge spectrum of HMCS-CT is shifted 鈭?.5 eV to lower energy compared to the pmARC-1 spectrum, which indicates that as-isolated HMCS-CT is in a more reduced state than pmARC-1. Extended X-ray absorption fine structure analysis indicates significant structural differences between pmARC-1 and HMCS-CT, with the former being a dioxo site and the latter possessing only a single terminal oxo ligand. The number of terminal oxo donors is consistent with pmARC-1 being in the Mo^VI oxidation state and HMCS-CT in the Mo^IV state. These structures are in accord with oxygen-atom-transfer reactivity for pmARC-1 and persulfide bond cleavage chemistry for HMCS-CT.