Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene (PubMed:2294092, PubMed:7037744, PubMed:10692370). Ferredoxin reductase catalyzes the transfer of electrons from NADH to ferredoxin (NdoA) (PubMed:2294092). NADPH is also effective but yields only 39% of the activity obtained with NADH (PubMed:2294092, PubMed:7037744). Also able to catalyze the cis-dihydroxylation of biphenyl and phenanthrene (PubMed:10692370). H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2 oxidized [2Fe-2S]-[ferredoxin] H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin] Binds 1 [2Fe-2S] cluster. Binds 1 mole of FAD per mole of enzyme. Also able to use FMN, but the activity is less than that obtained with FAD. Strongly inhibited by p-chloromercuribenzoate. Also inhibited by N-ethylmaleimide and o-phenanthroline. Aromatic compound metabolism; naphthalene degradation. The naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and a dioxygenase component (iron sulfur protein (ISP)). The electron transfer component is composed of a ferredoxin reductase (NdoR) and a ferredoxin (NdoA), and the dioxygenase component is formed of a heterohexamer (trimer of heterodimers) of three large alpha subunits (NdoB) and three small beta subunits (NdoC). Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase component family.