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. Author manuscript; available in PMC: 2011 Mar 30.
Published in final edited form as: Biochemistry. 2010 Mar 30;49(12):2725–2731. doi: 10.1021/bi100074s

Table 1.

Shifts in absorption band maxima in cm−1 relative to those in solution resulting from binding of naphthols in the pKSI active site and the fraction of the neutral species observed when bound. Errors indicate one standard deviation.

Ligand Protein Neutral shift Anionic shift Fraction neutral
Equilenin WT −280 ±17 446 ± 28 0.31 ± 0.02
Equilenin D40N −180 ± 14 730 ± 56 0.456 ± 0.005
6-bromo-2-naphthol D40N −475 ± 7 190 ± 28 0.32 ± 0.02
2,6-hydroxynaphthalene D40N −405 ± 63 1230 ± 212 0.71 ± 0.01
6-cyano-2-naphthol D40N −1480 ± 280 275 ± 7 0.08 ± 0.03
6-methoxy-2-naphthol D40N −390 ± 14 235 ± 7 0.54 ± 0.03