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. 2005 Feb;187(4):1511–1514. doi: 10.1128/JB.187.4.1511-1514.2005

TABLE 2.

Enhanced rates of oxidation of nitrophenols by the TouA E214 variantsa

Enzyme Substrate
o-Nitrophenol
p-Nitrophenol
Prod- uct Rateb Rela- tive Mol% Prod- uct Rateb Rela- tive Mol%
Wild-type ToMO 3-NC 0.12 ± 0.10 1.0 12 4-NC 0.0082 ± 0.0002 1.0 100
NHQ 0.95 ± 0.15 1.0 88
E214G/ D312N/ M399V 3-NC 0.28 2.4 14 4-NC 0.164 ± 0.002 20 100
NHQ 1.8 1.9 86
E214G 3-NC 0.25 ± 0.01 2.1 12 4-NC 0.124 ± 0.004 15 100
NHQ 1.9 ± 0.2 2.0 88
E214A 3-NC 0.19 1.6 14 4-NC 0.034 ± 0.001 4.3 100
NHQ 1.2 1.3 86
E214V 3-NC 0.14 1.2 16 4-NC 0.011 ± 0.001 1.3 100
NHQ 0.76 0.8 84
E214W 3-NC 0.038 ± 0.003 0.32 15 4-NC 0.0013 ± 0.0001 0.16 100
NHQ 0.21 ± 0.01 0.22 85
E214Q 3-NC 0.12 1.0 12 NM NM NM NM
NHQ 0.86 0.9 88
E214F 3-NC 0.09 0.8 12 NM NM NM NM
NHQ 0.74 0.8 88
a

o-Nitrophenol and p-nitrophenol initial concentrations were 500 μM. NM, not measured; 3-NC, 3-nitrocatechol; NHQ, nitrohydroquinone; 4-NC, 4-nitrocatechol. Products were identified via HPLC.

b

Initial rate, in nanomoles per minute per milligram of protein.