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. Author manuscript; available in PMC: 2012 Nov 1.
Published in final edited form as: FEBS J. 2011 Sep 15;278(21):4055–4069. doi: 10.1111/j.1742-4658.2011.08310.x

Fig 7. Patterns of enzyme distribution versus time for nNOSr reactions that were simulated using different rate pairings.

Fig 7

Rate pairs of conformational motion and interflavin electron transfer were chosen in each case to simulate an electron flux of 8 s-1. Lines indicate the relative concentrations of each enzyme species a-d (see Fig. 2), with the total enzyme concentration being 1.0 and the concentration of enzyme species d + a being set equal to 1.0 at time = 0 in the simulations. Dotted line marks the time required for nNOSr to reduce one equivalent of cytochrome c. Kinetic settings (s-1) were Panel A: k1 = k-1 = k3 = k-3= 17.5, k2 = 200; Panel B: k1 = k-1 = k3 = k-3= 34, k2 = 30; Panel C: k1 = k-1 = k3 = k-3= 45, k2 = 25; Panel D: k1 = k-1 = k3 = k-3= 80, k2 = 20.