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. 2010 May 12;285(29):21943–21950. doi: 10.1074/jbc.M110.117283

FIGURE 2.

FIGURE 2.

Characterization of lipoyl-dependent peroxidase activity. A, disulfide reductase activity of lipoamide systems. ●, 1 μm LpdA plus 0.5 μm PDHB; ♦, 1 μm Lpd plus 1 μm SucB; ■, 1 μm lipoamide plus 1 μm Lpd; ▴, 1 μm LpdA; □, 1 μm LpdA−LA; ▵, 1 μm Lpd plus 1 μm SucB−LA. −LA denotes proteins whose expression was not enriched with lipoic acid. B, lipoamide-dependent peroxidase activity of Cys-based thiol-dependent peroxidases (0.1 μm) in the presence of free lipoamide (0.2 mm), Lpd (0.5 μm), and t-BHP (0.2 mm). ●, Ohr; ▴, AhpC; ■, PrxQ; ♦, no further addition. C, Lineweaver-Burk plot of the lipoamide-dependent peroxidase activity of Ohr. Lipoamide concentrations were as follows: 7.5 μm (■), 10 μm (▴), and 15 μm (●). D, Henri-Michaelis-Menten plot for Ohr catalysis in reactions containing Ohr (1 μm), Lpd (5 μm), and lipoamide (0.1 mm). The result is the average of three independent experiments. Data are means ± S.D.