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

Fig 2

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. See text for details.