Figure 1 | Scientific Reports

Figure 1

From: Structural insights into the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas

Figure 1

The overall architecture of dimeric QFR from D. gigas. (a) The homo-dimer formed by two complexes of the subunits A (shown in green and brown), B (cyan and gray) and C (pink and purple) on the inner membrane. The redox cofactors, hemes, iron-sulphur clusters and FAD are shown by sticks. (b) Two homo-dimers formed by four sets of subunits A, B and C in the asymmetric unit. The FAD-binding domain (green), the capping domain (red), the helical domain (orange) and the C-terminal domain (yellow) of the subunit A are shown, respectively. The N-terminal plant-ferredoxin domain (red) and a C-terminal bacterial-ferredoxin domain (cyan) of the subunit B and the whole C subunit (pink) are shown.

Back to article page