EC Number |
Protein Variants |
Reference |
---|
1.7.1.3 | G811V |
site-directed mutagenesis, an FAD-binding mutant |
742843 |
1.7.1.3 | H654A/H677A |
site-directed mutagenesis, CD spectroscopy shows no negative effects of the introduced mutations on protein secondary structure in comparison to the wild-type protein, but the mutant contains no heme, while the FAD binding ability is not significantly disturbed |
742843 |
1.7.1.3 | more |
construction of null-mutants of gene niaD |
655066 |
1.7.1.3 | more |
different structural gene (niaD) and cofactor gene (cnx) mutants are analyzed concerning their flavin and molybdenum content |
395973 |
1.7.1.3 | more |
nit-1 mutant, suggested to produce the complete apoenzyme |
395978 |
1.7.1.3 | more |
nit-1 mutant: lacks all activities except FAD-dependent NADPH:cytochrome c reductase activity,nit-2 mutant: reduced FAD:- and reduced methyl viologen:nitrate reductase activities but lacks the other two activities |
395980 |
1.7.1.3 | more |
nit-3 mutant (FGSC 262): reduced FAD-nitrate reductase and reduced methylviologen-nitrate reductase activities |
395981 |
1.7.1.3 | more |
several mutations of recombinant cyt b reductase fragment of nitrate reductase in the region Ser920, Arg921 and Arg932 are created. Conversion from NADPH-specific to virtually NADH-specific cyt b reductase fragment of nitrate reductase |
395976 |
1.7.1.3 | more |
studies of temperature-sensitive mutations, niaD gene: mutation leads to loss of a 4.5-S cytochrome-c reductase activity, which is a subunit of nitrate reductase. It is suggested that neither the product of the cnxE nor the cnyF genes form part of the nitrate reductase molecule, but some catalytic role in cofactor formation, niaD and cnxH seem to be structural genes |
-, 395967 |
1.7.1.3 | more |
the purified native enzyme is successfully used for synthesis of silver nanoparticles in an NADPH-dependent manner using gelatin as a capping agent, analysis by X-ray diffraction, dynamic light scattering spectroscopy, and transmission and scanning electron microscopy, overview. 0.2 M Phosphate buffer, pH 7.2, 1 mM silver nitrate as the enzyme substrate, 0.1 mg gelatin as a capping agent, 1 mM 4-hydroxyquinoline as an electron carrier, 1 mM NADPH as enzyme cofactor, and 0.1 mg of purified fungal nitrate reductase are incubated at 25°C for 5 h. The stable nonaggregating nanoparticles are spherical in shape with an average size of 50 nm and a zeta potential of -34.3. The synthesized nanoparticles show a strong growth inhibitory antimicrobial activity against all tested human pathogenic fungi and bacteria, overview |
-, 741637 |