Engineering the Redox Potential over a Wide Range within a New Class of FeS Proteins

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• 作者：John A. Zuris ; Danny A. Halim ; Andrea R. Conlan ; Edward C. Abresch ; Rachel Nechushtai ; Mark L. Paddock ; Patricia A. Jennings
• 刊名：Journal of the American Chemical Society
• 出版年：2010
• 出版时间：September 29, 2010
• 年：2010
• 卷：132
• 期：38
• 页码：13120-13122
• 全文大小：187K
• 年卷期：v.132,no.38(September 29, 2010)
• ISSN：1520-5126

文摘

MitoNEET is a newly discovered mitochondrial protein and a target of the TZD class of antidiabetes drugs. MitoNEET is homodimeric with each protomer binding a [2Fe-2S] center through a rare 3-Cys and 1-His coordination geometry. Both the fold and the coordination of the [2Fe-2S] centers suggest that it could have novel properties compared to other known [2Fe-2S] proteins. We tested the robustness of mitoNEET to mutation and the range over which the redox potential (E_M) could be tuned. We found that the protein could tolerate an array of mutations that modified the E_M of the [2Fe-2S] center over a range of 700 mV, which is the largest E_M range engineered in an FeS protein and, importantly, spans the cellular redox range (+200 to −300 mV). These properties make mitoNEET potentially useful for both physiological studies and industrial applications as a stable, water-soluble, redox agent.