Addition/Correction Cite This: J. Am. Chem. Soc. XXXX, XXX, XXX-XXX
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Correction to “Identification of the TyrOH●+ Radical Cation in the Flavoenzyme TrmFO” Lipsa Nag, Pierre Sournia, Hannu Myllykallio, Ursula Liebl, and Marten H. Vos* J. Am. Chem. Soc. 2017, 139, 11500−11505. DOI: 10.1021/jacs.7b04586 Page 11501. In Figure 1, the label for residue Ser52 was placed at the wrong position, potentially confusing the description of the possible hydrogen bonds in the text. In the corrected Figure 1 (below), the label “S52” is replaced to clearly depict the position of this residue. We thank Dr. Klaus Brettel (CEA Saclay) for pointing out this mistake. This mistake does not change the conclusions of the paper in any way.
Figure 1. Structure of the active site of wild-type TrmFO (pdb 3G5Q). Red dots represent O atoms of structural water molecules. The thin dotted lines represent possible H-bonding interactions, using the standard relaxed H-bond constraints criteria of Chimera. The dashed line represents the distance between the Tyr343 O and the flavin N5 atoms. Distances are in Å.
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DOI: 10.1021/jacs.7b10508 J. Am. Chem. Soc. XXXX, XXX, XXX−XXX
