recombinant truncated NOR exhibits the same spectroscopic properties and reactivity to NO and O2 as wil-type NOR, although its enzymatic activity toward NO is considerably decreased
reduction of NO to N2O by denitrifiying bacteria is catalyzed either by a monomeric quinol-nitric oxide reductase (qNor, EC 1.7.5.2) or by a heterodimeric cytochrome c-dependent nitric oxide reductase (cNor), composed of three subunits encoded on single genes in one cotranscribed gene cluster, direct interactions between NorH and the NorCB complex. NOR are the main enzymes involved in the reduction of NO during the denitrification process
reduction of NO to N2O by denitrifiying bacteria is catalyzed either by a monomeric quinol-nitric oxide reductase (qNor, EC 1.7.5.2) or by a heterodimeric cytochrome c-dependent nitric oxide reductase (cNor), composed of three subunits encoded on single genes in one cotranscribed gene cluster, direct interactions between NorH and the NorCB complex. NOR are the main enzymes involved in the reduction of NO during the denitrification process
membrane-integrated nitric oxide reductase (NOR) is an iron-containing enzyme involved in the denitrification process and catalyzes the reduction of nitric oxide (NO) to nitrous oxide (N2O) with two protons and two electrons via cleavage of the N-O bond and concomitant formation of the N-N bond. No proton transfer pathway occurs from the inside of the membrane, but via two water channels, involving residue Asp198 in channel 1 of Pseudomonas aeruginosa cNOR, channel structure analysis, overview
Halomonas halodenitrificans nitric oxide reductase (NOR) is the membrane-bound heterodimer complex of NorC, which contains a low-spin heme c center, and NorB, which contains a low-spin heme b center, a high-spin heme b3 center, and a non-heme FeB center
Halomonas halodenitrificans nitric oxide reductase (NOR) is the membrane-bound heterodimer complex of NorC, which contains a low-spin heme c center, and NorB, which contains a low-spin heme b center, a high-spin heme b3 center, and a non-heme FeB center
quantum chemical calculations and combination of computational and experimental data for analysis of the reduction of nitric oxide (NO) to nitrous oxide and water in the membrane enzyme, cytochrome c dependent nitric oxide reductase (cNOR). Binuclear active site modelling and structure of the cis-hyponitrite intermediate, overview
structure-based molecular dynamics simulation, overview. Active site located essential residue Glu211 of cNOR. Three conserved glutamate residues locate at the close proximity to the active site and forms a small hydrophilic cavity