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Literature summary extracted from
- Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A (2003), Nat. Struct. Biol., 10, 681-687.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.7.5.1 | crystal structure of NarGHI at 1.9 A resolution, crystals of native and selenomethionine-substituted NarGHI are obtained by vapor diffusion with sitting drops | Escherichia coli |
| 1.7.5.1 | sitting-drop vapor diffusion method, crystals of native and selenomethionine-substituted NarGHI, crystal structure at 1.9 A resolution | Escherichia coli |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.7.5.1 | cytoplasm | NarG and NarH are cytoplasmic subunits | Escherichia coli | 5737 | - |
| 1.7.5.1 | cytoplasmic membrane | the transmembrane subunit NarI anchors narGH to the cytoplasmic side of the membrane | Escherichia coli | - |
- |
| 1.7.5.1 | membrane | the membrane-intrinsic subunit NarI anchors NarGH to the membrane through a predominantly hydrophobic interface with both subunits | Escherichia coli | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.7.5.1 | Fe | domain I of subunit NarG holds the [4Fe-4S] cluster FS0. The coordination scheme of FS0 is: His50, Cys54, Cys58, Cys93. NarH contains three [4Fe-4S] clusters, FS1, FS2, FS3 and one [3Fe-4S] cluster, FS4 | Escherichia coli |  |
| 1.7.5.1 | Fe | domain I of the catalytic subunit NadG holds the [4Fe-4S] cluster FS0 | Escherichia coli | |
| 1.7.5.1 | Mo | the enzyme uses a molybdo-bis(molybdopterin guanine dinucleotide) cofactor for catalytic mechanism | Escherichia coli | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.7.5.1 | 223900 | - |
multiple isomorphous replacement and anaomalous scattering (MIRAS), crystallographic data | Escherichia coli |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.7.5.1 | nitrate + quinol | Escherichia coli | nitrate reductase A reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force | nitrite + quinone + H2O | - |
? | |
| 1.7.5.1 | nitrate + quinol | Escherichia coli | under anaerobic conditions in the presence of nitrate, Escherichia coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (nitrate reductase A, NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. The arrangement, coordination scheme and unique environment of the redox-active prosthetic groups is revealed | nitrite + quinone + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.7.5.1 | Escherichia coli | - |
- |
- |
| 1.7.5.1 | Escherichia coli | P11349 and P09152 and P11350 | narH: P11349, narG: P09152, narI: P11350 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.7.5.1 | - |
Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.7.5.1 | nitrate + 2-methyl-1,4-naphthoquinol | i.e. menadiol | Escherichia coli | nitrite + 2-methyl-1,4-naphthoquinone + H2O | - |
? | |
| 1.7.5.1 | nitrate + quinol | nitrate reductase A reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force | Escherichia coli | nitrite + quinone + H2O | - |
? | |
| 1.7.5.1 | nitrate + quinol | under anaerobic conditions in the presence of nitrate, Escherichia coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (nitrate reductase A, NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. The arrangement, coordination scheme and unique environment of the redox-active prosthetic groups is revealed | Escherichia coli | nitrite + quinone + H2O | - |
? | |
| 1.7.5.1 | nitrate + ubiquinol | - |
Escherichia coli | nitrite + ubiquinone + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.7.5.1 | heterotrimer | electron transfer can occur from the menaquinol binding site in NarI to the molybdo-bis(molybdopterin guanine dinucleotide) active site in NarG, where nitrate is reduced to nitrite | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.7.5.1 | NarGHI | - |
Escherichia coli |
| 1.7.5.1 | nitrate reductase A | - |
Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.7.5.1 | bis(molybdopterin guanine dinucleotide)molybdenum cofactor | structural evidence for the role of an open bicyclic form of the molybdo-bis(molybdopterin guanine dinucleotide) cofactor in the catalytic mechanism | Escherichia coli | |
| 1.7.5.1 | bis(molybdopterin guanine dinucleotide)molybdenum cofactor | the enzyme uses a molybdo-bis(molybdopterin guanine dinucleotide) cofactor for catalytic mechanism | Escherichia coli | |
| 1.7.5.1 | heme | the transmembrane subunit NarI coordinates two low-spin hemes, heme bP and heme bD, which mediate electron transfer from the Q-site to the [Fe-S] clusters in NarH | Escherichia coli | |
| 1.7.5.1 | additional information | the transmembrane subunit NarI provides the quinol binding and oxidation site (Q-site) | Escherichia coli |
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