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  • A simple method to engineer a protein-derived redox cofactor for catalysis.

A simple method to engineer a protein-derived redox cofactor for catalysis.

Biochimica et biophysica acta (2014-05-27)
Sooim Shin, Moonsung Choi, Heather R Williamson, Victor L Davidson
摘要

The 6×-Histidine tag which is commonly used for purification of recombinant proteins was converted to a catalytic redox-active center by incorporation of Co(2+). Two examples of the biological activity of this engineered protein-derived cofactor are presented. After inactivation of the natural diheme cofactor of MauG, it was shown that the Co(2+)-loaded 6×His-tag could substitute for the hemes in the H2O2-driven catalysis of tryptophan tryptophylquinone biosynthesis. To further demonstrate that the Co(2+)-loaded 6×His-tag could mediate long range electron transfer, it was shown that addition of H2O2 to the Co(2+)-loaded 6×His-tagged Cu(1+) amicyanin oxidizes the copper site which is 20Å away. These results provide proof of principle for this simple method by which to introduce a catalytic redox-active site into proteins for potential applications in research and biotechnology.

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色氨酸 -L, reagent grade, ≥98% (HPLC)
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色氨酸 -L, from non-animal source, meets EP, JP, USP testing specifications, suitable for cell culture, 99.0-101.0%
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色氨酸, Pharmaceutical Secondary Standard; Certified Reference Material
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色氨酸 -L, certified reference material, TraceCERT®
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