Any feedback?
Literature summary for 1.7.5.1 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)
| Crystallization (Comment) | Organism |
|---|---|
| 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 |
| sitting-drop vapor diffusion method, crystals of native and selenomethionine-substituted NarGHI, crystal structure at 1.9 A resolution | Escherichia coli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoplasm | NarG and NarH are cytoplasmic subunits | Escherichia coli | 5737 | - |
| cytoplasmic membrane | the transmembrane subunit NarI anchors narGH to the cytoplasmic side of the membrane | Escherichia coli | - |
- |
| membrane | the membrane-intrinsic subunit NarI anchors NarGH to the membrane through a predominantly hydrophobic interface with both subunits | Escherichia coli | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 |  |
| Fe | domain I of the catalytic subunit NadG holds the [4Fe-4S] cluster FS0 | Escherichia coli | |
| Mo | the enzyme uses a molybdo-bis(molybdopterin guanine dinucleotide) cofactor for catalytic mechanism | Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 223900 | - |
multiple isomorphous replacement and anaomalous scattering (MIRAS), crystallographic data | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
| Escherichia coli | P11349 and P09152 and P11350 | narH: P11349, narG: P09152, narI: P11350 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| nitrate + 2-methyl-1,4-naphthoquinol | i.e. menadiol | Escherichia coli | nitrite + 2-methyl-1,4-naphthoquinone + H2O | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| nitrate + ubiquinol | - |
Escherichia coli | nitrite + ubiquinone + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| NarGHI | - |
Escherichia coli |
| nitrate reductase A | - |
Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 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 | |
| bis(molybdopterin guanine dinucleotide)molybdenum cofactor | the enzyme uses a molybdo-bis(molybdopterin guanine dinucleotide) cofactor for catalytic mechanism | Escherichia coli | |
| 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 | |
| additional information | the transmembrane subunit NarI provides the quinol binding and oxidation site (Q-site) | Escherichia coli |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
