TABLE 1.
Characteristic | Assimilatory, NO3− assimilation | Dissimilatory
|
|
---|---|---|---|
NO3− respiration | NO3− reduction | ||
Nitrate reductase | Assimilatory Nas | Respiratory Nar | Dissimilatory Nap |
Location | Cytoplasm | Membrane | Periplasm |
Reaction catalyzed | NO3−⇒NO2− | NO3−⇒NO2− | NO3−⇒NO2− |
Structural genes | nasCAa/narBb | narGHI | napAB |
Prosthetic groups | FADc, FeSd, MGD | cytbe, FeS, MGD | cytc, FeS, MGD |
Nitrate transport | Yes | Yes | No |
Function | Biosynthesis of N compounds | PMF (nitrate respiration and denitrification) | 2H ⇓f and denitrification |
Regulationg | |||
O2 | No | Yes | No/yes |
NH4+ | Yes | No | No |
NO3−/NO2− | Yes | Yes | No/yes |
Following the gene designation in K. oxytoca for the NADH-nitrate reductase.
Following the gene designation in cyanobacteria for the ferredoxin-nitrate reductase.
FAD is present in the diaphorase subunit of the NADH-dependent nitrate reductases, but it is absent from the cyanobacterial ferredoxin-nitrate reductase.
FeS, iron-sulfur centers.
cytb, cytochrome b.
2H⇓, dissipation of reducing power. A PMF can be generated if a proton-translocating complex is involved in the electron transfer, but in most cases, this seems to be insufficient to support ATP synthesis coupled to nitrate reduction.
Some differences in regulation in prokaryotic organisms have been reported.