Crystallization (Comment) | Organism |
---|---|
X-ray diffraction structure analysis, resolution 2.2 A, PDB ID 2jio, modelling | Desulfovibrio desulfuricans |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Desulfovibrio desulfuricans | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | in the heme/cytochrome cofactor | Desulfovibrio desulfuricans | |
Mo(VI) | coordinates a cysteine and a sulfido residue | Desulfovibrio desulfuricans |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ferrocytochrome + 2 H+ + nitrate | Desulfovibrio desulfuricans | - |
2 ferricytochrome + nitrite | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Desulfovibrio desulfuricans | P81186 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O | sulfur-shift mechanism catalytic mechanism. The second sphere type of mechanism is supported by the recent X-ray structures of Nap from Desulfovibrio desulf uricans ATCC 27774 and Cupriavidus necator H16, in which the sixth sulfur ligand of the Mo interacts with the sulfur from the cysteine residue and generates a bidentate persulfido ligand that sterically blocks the access of the substrate to the Mo ion, modelling | Desulfovibrio desulfuricans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ferrocytochrome + 2 H+ + nitrate | - |
Desulfovibrio desulfuricans | 2 ferricytochrome + nitrite | - |
? |
Synonyms | Comment | Organism |
---|---|---|
NAP | - |
Desulfovibrio desulfuricans |
periplasmic nitrate reductase | - |
Desulfovibrio desulfuricans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome c | - |
Desulfovibrio desulfuricans | |
molybdenum cofactor | a Mo-pyranopterin cofactor | Desulfovibrio desulfuricans |
General Information | Comment | Organism |
---|---|---|
evolution | the periplasmic nitrate reductase (Nap) from Desulfovibrio desulfuricans belongs to the DMSO reductase family, subfamily I. Classification of Mo-pyranopterin dependent enzymes from the DMSO reductase family, e.g. periplasmic nitrate reductase and formate dehydrogenase, overview. Comparison of the sulfur-shift mechanism in nitrate reductase (Nap) and in formate dehydrogenase (Fdh), detailed overview | Desulfovibrio desulfuricans |