F420H(2)-dependent reductase able to catalyze the reduction of biliverdin-IXalpha to bilirubin-IXalpha in vitro. However, kinetic parameters show that it is less efficient than the biliverdin reductase Rv2074 and suggest biliverdin-IXalpha is unlikely to be the native substrate of Rv1155, which probably catalyzes the reduction of an alternative molecule in vivo (PubMed:27364382). Binds coenzyme F420, but does not bind FMN or other flavins (PubMed:25644473). Cannot use pyridoxine 5'-phosphate, pyridoxamine 5'-phosphate, pyridoxal 5'-phosphate (PLP), the anti-tuberculosis drug PA-824 or aflatoxin analogs as substrates (PubMed:25644473). kcat is 0.024 sec(-1) for the reduction of biliverdin. Homodimer. Belongs to the F420H(2)-dependent biliverdin reductase family. Was originally thought to be an FMN-dependent pyridoxine 5'-phosphate oxidase. FMN and PLP are seen in the crystal structures published in PubMed:16239726, however, the enzyme does not bind these compounds in vitro, and the complexes obtained in the crystal structures may be the result of weak FMN/PLP binding that is stabilized by the crystal lattice.