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The nitroreductase of Enterobacter cloacae was identified by Bryant and Deluca in E. cloaca isolated from a munitions facility, on the basis of its ability to metabolize TNT (trinitrotoluene). Since then many homologues have been identified and the family is now known to include members in diverse organisms, that catalize diverse reactions. The iodotyrosine deiodenase of mammals is a dehalogenase, the BluB of Sinorhizobium meliloti canibalizes the bound FMN to furnish a critical intermediate in vitamin B12 biosynthesis.

Crystal structures of the E. cloacae and E. coli enzymes have been published with a variety of substrates and analogues bound.

Mechanism: the nitroreductase of E. cloaca was shown to employ ping-pong bi-bi mechanism. This was confirmed for E. coli by Race et al.