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. Author manuscript; available in PMC: 2021 Aug 23.
Published in final edited form as: ACS Catal. 2020 Jun 23;10(13):7413–7418. doi: 10.1021/acscatal.0c01885

Figure 3.

Figure 3.

Deuteration of arginine-related substrates. (A) α-deuterated compound formation. (B) Potential mechanisms of proton/deuterium transfers in SxtA AONS. (C) Timecourse of α-deuteration by mass spectrometry. (D) Comparison of deuterium incorporation and enantiomeric composition when starting with l-Arg-OMe (blue) or d-Arg-OMe (red). (E) 1H NMR of l-Arg-OMe (l-13) incubated with AONS over 30 min, confirming exchange of the α-proton to deuterium (see SI for conditions). Peaks present between 3.7−3.5 ppm are attributed to glycerol from the enzyme storage buffer.