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. 2004 Jul;70(7):3814–3820. doi: 10.1128/AEM.70.7.3814-3820.2004

TABLE 2.

Synthesis of phenol from benzene, catechol from phenol, and 1,2,3-THB from catechol by E. coli TG1 cells expressing wild-type T4MO, T3MO, and TOMa

Enzyme Phenol formation from benzene
Catechol formation from phenol
1,2,3-THB formation from catechol
Toluene oxidation rate (nmol/min/mg protein)
Initial formation rate (nmol/min/mg of protein) Maximum production (μM) Initial formation rate (nmol/min/mg of protein) Maximum production (μM) Initial formation rate (nmol/min/mg protein) Maximum production (μM)
T4MOb 19 ± 1.6 144 ± 47 13.6 ± 0.3 103 ± 10 2.5 ± 0.5 132 ± 22 10 ± 0.8
T3MOb 3 ± 1 122 ± 43 3.1 ± 0.3 119 ± 13 0.26 ± 0.09 73 ± 4 4 ± 0.6
TOMc 0.89 ± 0.07 27 ± 12 1.8 ± 0.5 140 ± 7 1.7 ± 0.3 103 ± 22 2.4 ± 0.3
a

As determined on the basis of HPLC analysis, the means ± standard deviations of at least two independent results are shown. The initial benzene liquid concentration was 165 μM on the basis of a Henry's law constant of 0.22 (9) (a 400 μM concentration was added as if all the benzene was in the liquid phase), and the initial toluene concentration was 165 μM on the basis of a Henry's law constant of 0.27 (9) (a 455 μM concentration was added as if all the toluene was in the liquid phase).

b

Protein concentration, 0.24 mg of protein/ml·OD.

c

Protein concentration, 0.22 mg of protein/ml·OD.