Fig. 2: The electron transfer pathway in RcFDH. | Nature Communications

Fig. 2: The electron transfer pathway in RcFDH.

From: Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase

Fig. 2

a Overall layout and location of cofactors in RcFDH. The distances between redox centres are given in angstroms, for both centre-to-centre and edge-to-edge (shown in parentheses) measurements. Fe-S clusters are named according to their position in the electron transfer chain and the RcFDH subunit they are located in. The inset depicts the location of the cofactor in the atomic model of RcFDH. b Layout and location of cofactors in subunits Nqo1-3 of the hydrophilic domain of TtRC I (PDB-ID: 3iam [https://doi.org/10.2210/pdb3IAM/pdb]) depicted in the same orientation as RcFDH in (a). Colour code is as follows I: Nqo1, red; Nqo2, blue; Nqo3, green. c The FdsA C-terminus (red) forms a cap domain interacting with proximal and distal MGD as well as FdsD (yellow). Cofactors are shown as spheres. Important interacting amino acids in FdsA and FdsD are indicated and shown in stick representation. d Multiple sequence alignment of extended loop in FdsA homologues from organisms with predicted FdsD (grey-shaded) or without predicted FdsD (white-shaded). In Methanothermobacter wolfeii the C-terminus of FdsA is replaced by an additional subunit with low homology in the extended loop. The star indicates the position of the conserved Trp residue in NAD+ dependent FDHs.

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