Rhodoquinone (RQ) is a modified ubiquinone-like molecule that is an important cofactor used in anaerobic energy metabolism by many organisms.

Recently, it has gained attention as a potential anthelmintic drug target due to the fact that parasitic hosts do not synthesize or use this cofactor.

[5][6] The RquA protein uses S-adenosyl-L-methionine as the amino donor to convert UQ to RQ in an unusual Mn(II)-catalyzed reaction.

With this proposed biosynthesis, the kynurenine pathway still needs to be upregulated, and activity from certain genes like kynu-1 which encodes for the KYNU-1 enzyme that catalyzes production of 3-hydroxy-L-kynurenine to 3-hydroxyanthranilic acid, needs to be upheld.

[8][9] Recent work has revealed that alternative splicing of the coq-2 polyprenyltransferase gene controls the level of RQ in animals.