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. Author manuscript; available in PMC: 2015 Dec 1.
Published in final edited form as: FEBS J. 2014 Oct 25;281(23):5325–5340. doi: 10.1111/febs.13073

Figure 1. Kinetic model for electron flux through a dual-flavin enzyme.

Figure 1

The model uses four kinetic rates: association (k1 or k3) and dissociation (k−1 or k−3) of the FMN and FNR domains; the FMNH• reduction rate (k2), and the cytochrome c reduction rate (k4). The fully-reduced enzyme in the open conformation (species a) reduces cytochrome c and generates species b, which then undergoes successive conformational closing, interflavin electron transfer, and conformational opening steps to complete the cycle.