Naphthalene 1,2-dioxygenase (NDO)

Naphthalene 1,2-dioxygenase (NDO) is a multicomponent enzyme system found in various soil bacteria, most notably Pseudomonas putida, where it catalyzes the first step in the aerobic degradation of naphthalene (UniProt: P0A114). It belongs to the Rieske non-heme iron dioxygenase family and is responsible for the stereospecific cis-dihydroxylation of the aromatic ring to form (1R,2S)-1,2-dihydronaphthalene-1,2-diol (PubMed: 9630217). The enzyme complex consists of a reductase, a ferredoxin, and an alpha-3-beta-3 heterohexameric oxygenase that contains both a Rieske [2Fe-2S] cluster and a mononuclear non-heme iron active site (PubMed: 11514513). While NDO is not a target for human therapeutic intervention, it is highly valued in biotechnology for its broad substrate specificity, allowing for the bioremediation of environmental pollutants and the biocatalytic synthesis of chiral chemicals and dyes such as indigo (PubMed: 6314503). Its ability to incorporate both atoms of molecular oxygen into a wide range of polycyclic aromatic hydrocarbons makes it a model system for studying oxygen activation and electron transfer in metalloenzymes.

Other names

Naphthalene dioxygenaseNDONaphthalene 1,2-hydroxylase

Not applicable for therapeutic drugs; the enzyme catalyzes the stereospecific cis-dihydroxylation of naphthalene using a Rieske [2Fe-2S] center and a mononuclear iron active site (PubMed: 11514513).