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. Author manuscript; available in PMC: 2016 Feb 3.
Published in final edited form as: Biochemistry. 2015 Jan 17;54(4):1043–1052. doi: 10.1021/bi501350j

Figure 6. Redox-dependent interplay between the g =1.91 and g = 1.92 components of the [2Fe-2S] cluster EPR spectrum.

Figure 6

The height differentials between the g = 1.91 and g = 1.92 components of the [2Fe-2S] cluster EPR signal as a function of ambient potential were plotted for wild-type SdhCDAB (black), SdhA-H45A (green), SdhA-R286A (yellow), and SdhA-R286K (blue) and fitted to the Nernst equation. For titration of the wild-type SdhCDAB enzyme, a second component corresponding to the reduction of the [2Fe-2S] cluster itself was also modeled.