FIG 6.

Amino acid sequence alignments of α- and β-subunits of CumDO Oxy with those of α₃β₃-type Oxys coupled with Rieske-type Fds. Only the parts of Oxy including the potential important amino acid residues for binding to Rieske-type Fds are shown. Conserved and similar amino acid residues at positions crucial for binding between α₃β₃-type Oxys and Rieske-type Fds (indicated by arrowheads) are darkly and lightly shaded, respectively. Four ligands for the Rieske cluster in α subunits are underlined. Numbers at right show the positions of terminal amino acid residues. Enzyme names followed by origins (subscripted) are shown at left.