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. 2006 Jan 9;103(3):708–713. doi: 10.1073/pnas.0506562103

Fig. 4.

Fig. 4.

Apparent IC50 for NO as a function of enzyme turnover at different [O2]. (A) Points represent experimental data, error bars represent 95% confidence limit, and solid lines are theoretical fits obtained by using the model and associated equation proposed by Antunes et al. (43): IC50 = Ki (1 + kO2app/kiv [O2]), where Ki = 0.2 nM, kiv is the turnover number in units of e s–1aa3–1, and kO2app was calculated according to Verkhovsky et al. (53). (Inset) the residual obtained after subtracting the theoretical fits from the actual data (•, 150 μM O2; □, 122 μM O2; ⋄, 88 μM O2; ▴, 49 μM O2). (B) The same data points with solid fit lines corresponding to our model; equation and values are shown in Fig. 3 and its legend (error bars represent SEM). A model in which NO interacts with the binuclear center in both oxidized and reduced states clearly fits the data more closely than does the simple competitive model.