The evolution of substrate specificity-associated residues and Ca2+-binding motifs in EF-hand-containing type II NAD(P)H dehydrogenases
Most eukaryotic organisms, except some animal clades, have mitochondrial alternative electron transport enzymes that allow respiration to bypass the energy coupling in oxidative phosphorylation. The energy bypass enzymes in plants include the external type II NAD(P)H dehydrogenases (DHs) of the NDB family, which are characterized by an EF-hand domain for Ca2+ binding. Here we investigate these pla
