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. Author manuscript; available in PMC: 2019 Feb 20.
Published in final edited form as: Biochemistry. 2018 Jan 31;57(7):1178–1189. doi: 10.1021/acs.biochem.7b01132

Figure 8.

Figure 8

Lipoamide Dehydrogenase: structure, reactions and probe design. Panel A shows the three dimensional structure of S. cerevisiae lipoamide dehydrogenase (PDB: 1V59). The two subunits of this homodimer are depicted in green and grey and bound FAD, redox active disulfide, and NAD+ cofactors are shown as space-filling representations colored yellow, magenta, and blue respectively. Panel B shows the reductive and oxidative half reactions without regard to protonation states of the reactants and products. The flavin and redox active disulfide moieties of the dehydrogenase lie within the white box. Panel C is a schematic depiction of the fusion protein attached to the mCherry fluorescent protein (PDB: 2H5Q).