EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
    1.7.2.5 | nitrous oxide + 2 ferricytochrome c + H2O |
- |
Pseudomonas aeruginosa |
2 nitric oxide + 2 ferrocytochrome c + 2 H+ |
- |
? |
| 1.7.2.5 | more |
both toxin Dtx and nitric oxide reductase are the two key players required for survival and pathogenesis of Corynebacterium diphtheriae, their expressions being controlled by two independent regulators DtxR and DIP1512 respectively. The controlling system appears to be decoupled because of differential affinities of the two regulators for NO |
Corynebacterium diphtheriae |
? |
- |
? |
| 1.7.2.5 | more |
Pseudomonas aeruginosa NO reductase may contribute to the intracellular survival by acting as a counter component against the hostยs defense systems |
Pseudomonas aeruginosa |
? |
- |
? |
| 1.7.2.5 | more |
the dissimilative nitrate respiration regulator DNR is involved in transcription regulation of the enzyme, apo-DNR binds heme in vitro and the heme-bound form reacts with carbon monoxide and NO, thus supporting the hypothesis that NO sensing involves gas binding to the ferrous heme, mechanism and structure, overview |
Pseudomonas aeruginosa |
? |
- |
? |
| 1.7.2.5 | more |
all-atom molecular dynamics simulations within an explicit membrane/solvent environment reveal two possible proton transfer pathways leading from the periplasm to the active site, while no pathways from the cytoplasmic side are found, consistently with the experimental observations that the enzyme is not a proton pump. One of the pathways is blocked in the crystal structure and requires small structural rearrangements to allow for water channel formation. That pathway is equivalent to the functional periplasmic cavity postulated in cbb3 oxidase |
Pseudomonas aeruginosa |
? |
- |
? |
| 1.7.2.5 | more |
quantumchemical calculations show that the reduction of the NO molecules by the enzyme and the formation of N2O are very exergonic steps, making the rereduction of the enzyme endergonic and rate-limiting for the entire catalytic cycle. Therefore the NO reduction cannot be electrogenic, i.e. cannot take electrons and protons from the opposite sides of the membrane, since it would increase the endergonicity of the rereduction when the gradient is present, thereby increasing the rate-limiting barrier, and the reaction would become too slow. It also means that proton pumping coupled to electron transfer is not possible in cytochrome c-dependent nitric oxide reductase |
Pseudomonas aeruginosa |
? |
- |
? |
| 1.7.2.5 | more |
NO reduction takes place in the NorB subunit that contains three redox centers: two b-type hemes (hemes b and b3) and a non-heme iron (FeB). Heme b3 and the non-heme iron form the binuclear center, where nitric oxide is bound and reduced. Determination of reduction rates of the cNOR variants with O2 and NO |
Paracoccus denitrificans |
? |
- |
? |
| 1.7.2.5 | more |
all-atom molecular dynamics simulations within an explicit membrane/solvent environment reveal two possible proton transfer pathways leading from the periplasm to the active site, while no pathways from the cytoplasmic side are found, consistently with the experimental observations that the enzyme is not a proton pump. One of the pathways is blocked in the crystal structure and requires small structural rearrangements to allow for water channel formation. That pathway is equivalent to the functional periplasmic cavity postulated in cbb3 oxidase |
Pseudomonas aeruginosa ATCC 15692 |
? |
- |
? |
| 1.7.2.5 | O2 + reduced cytochrome c |
- |
Paracoccus denitrificans |
H2O + cytochrome c |
- |
? |
| 1.7.2.5 | O2 + reduced acceptor + H+ |
- |
Paracoccus denitrificans |
H2O + oxidized acceptor |
- |
? |
