Guiding an enzyme all around a ring

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Science  05 Jan 2018:
Vol. 359, Issue 6371, pp. 44
DOI: 10.1126/science.359.6371.44-c

Most compounds of interest for pharmaceuticals, agrochemicals, and cosmetics have many C–H bonds, interspersed with a few carbon bonds to heavier elements that give them their distinct properties. Chemists therefore prize methods that let them selectively modify a variety of C–H bonds. Gilbert et al. report a versatile strategy that relies on a tethered amine to steer an engineered cytochrome P450 enzyme around 11- or 12-membered rings, transforming specific C–H bonds into C–O bonds. Subtle structural variation of the tether through click chemistry tunes the site selectivity.

ACS Cent. Sci. 10.1021/acscentsci.7b00450 (2017).

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