A bimodal imaging probe FCy7-NO2 was applied to image nitroreductase overexpressed by lung cancer in vivo, as reported Xin Zhou and co-workers their Research Article (e202213495). Integrating two complementary technologies into enables sensitive detection of over a broad concentration range without tissue-depth limit.

A highly sensitive and selective nitroreductase probe, showing a rapid and strong bioluminescence enhancement (>100-fold in 5 minutes), and its initial application in the real time detection of both Gram positive and Gram negative live bacteria and monitoring of their growth has been reported.

NfsB is an oxygen-insensitive nitroreductase of Escherichia coli with significant amino acid sequence homology to the major flavin reductase (FRase I) of Vibrio fischeri. Here, we show that NfsB is convertible to an FRase I-like flavin reductase three times as active as the authentic FRase I by a single amino acid substitution in the least-conserved region.

With this research we set out to develop a coumarin-based novel fluorescent probe NTR-AHC for the detection of biological thiols and nitroreductase (NTR). Probe was constructed by attaching NTR trigger moiety (p-nitrobenzyl) biothiol acceptor (maleic acid monoamide), core fluorophore AHC. In presence both glutathione (GSH) NTR, produced >8-fold increase in fluorescence intensity at 463 nm.

A novel long-wavelength fluorescence probe has been developed for the detection of nitroreductase (NTR) and hypoxia. could be activated by NTR at 0.1 μM to release the fluorophore and significant changes in fluorescence emission at 658 nm were observed. This feature makes it advantageous for imaging hypoxic cells with minimal endogenous interference.

Pseudomonas pseudoalcaligenes JS52 grows on nitrobenzene via partial reduction of the nitro group and enzymatic rearrangement of the resultant hydroxylamine. Cells and cell extracts of nitrobenzene-grown JS52 catalyzed the transient formation of 4-hydroxylamino-2,6-dinitrotoluene (4HADNT), 4-amino-2,6-dinitrotoluene (4ADNT), and four previously unidentified metabolites from 2,4,6-trinitrotoluen...

The protonation state of the deazaflavin dependent nitroreductase (Ddn) enzyme bound cofactor F420 was investigated using UV-visible spectroscopy and computational simulations. The reduced cofactor F420H2 was determined to be present in its deprotonated state in the holoenzyme form. The mechanistic implications of these findings are discussed.

A new bacterial nitroreductase has been identified and used as a biocatalyst for the controllable reduction of a variety of nitroarenes with an electron-withdrawing group to the corresponding N-arylhydroxylamines under mild reaction conditions with excellent selectivity (>99%). This method therefore represents a green and efficient method for the synthesis of arylhydroxylamines.