A dramatic switch of reactivity — from hydroquinone oxidation to N-hydroxylation — can be achieved through the rational engineering of a de novo-designed di-iron protein. Four specific amino-acid mutations spread throughout the first, second and third coordination shells result in a million-fold increase in the relative rate of these two reactions.
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References
Nanda, V. & Koder, R. L. Nature Chem. 2, 15–24 (2010).
Lu, Y., Yeung, N., Sieracki, N. & Marshall, N. M. Nature 460, 855–862 (2009).
Reig, A. J. et al. Nature Chem. 4, 900–906 (2012).10.1038/nchem.1454
Sazinsky, M. H. & Lippard, S. J. Acc. Chem. Res. 39, 558–566 (2006).
Kurtz, D. M. Jr J. Biol. Inorg. Chem. 2, 159–167 (1997).
Zocher, G., Winkler, R., Hertweck, C. & Schulz, G. E. J. Mol. Biol. 373, 65–74 (2007).
Calhoun, J. R. et al. J. Mol. Biol. 334, 1101–1115 (2003).
Lombardi, A. et al. Proc. Natl Acad. Sci. USA 97, 6298–6305 (2000).
Calhoun, J. R. et al. Structure 16, 210–215 (2008).
Guy, J. E. et al. Proc. Natl Acad. Sci. USA 103, 17220–17224 (2006).
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Berry, S. Engineering di-iron enzymes. Nature Chem 4, 868–869 (2012). https://doi.org/10.1038/nchem.1483
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DOI: https://doi.org/10.1038/nchem.1483
