Literature summary extracted from
Sakurai, N.; Kataoka, K.; Sugaya, N.; Shimodaira, T.; Iwamoto, M.; Shoda, M.; Horiuchi, H.; Kiyono, M.; Ohta, Y.; Triwiyono, B.; Seo, D.; Sakurai, T.
Heterologous expression of Halomonas halodenitrificans nitric oxide reductase and its N-terminally truncated NorC subunit in Escherichia coli (2017), J. Inorg. Biochem., 169, 61-67 .
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
1.7.2.5 |
gene norC, recombinant expression of wild-type and mutant NorC subunits in Escherichia coli strain BL21(DE3) |
Halomonas halodenitrificans |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
1.7.2.5 |
additional information |
construction of a truncated soluble domain of NorC, NorC* (DELTAMet1-Val37), by deletion of the 84 5'-terminal nucleotides of gene norC. The mutant NorC exhibits spectra typical of a low-spin heme c. In addition, NorC* functions as the acceptor of an electron from a cytochrome c isolated from the periplasm of Halomonas halodenitrificans and small reducing reagents. The redox potential of NorC* shifted ca. 40mV in the negative direction from that of wild-type NorC. Recombinant NOR exhibits the same spectroscopic properties and reactivity to NO and O2 as wil-type NOR, although its enzymatic activity toward NO is considerably decreased |
Halomonas halodenitrificans |
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
1.7.2.5 |
inner membrane |
NorB is themembrane-spanning subunit |
Halomonas halodenitrificans |
- |
- |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.7.2.5 |
Fe2+ |
subunit NorB contains a low-spin heme b center, a high-spin heme b3 center, and a non-heme FeB center |
Halomonas halodenitrificans |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.7.2.5 |
Halomonas halodenitrificans |
O50651 |
small subunit encoded by gene norC; formerly Paracoccus halodenitrificans |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
1.7.2.5 |
recombinant wild-type and mutant NorC subunits from Escherichia coli strain BL21(DE3) by anion exchange chromatography, gel filtration, and again ion exchange chromatography |
Halomonas halodenitrificans |
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.7.2.5 |
heterodimer |
membrane-bound heterodimer complex of NorC, which contains a low-spin heme c center, and NorB, which contains a low-spin heme b center, a high-spin heme b3 center, and a non-heme FeB center. NorB is themembrane-spanning subunit, it contains 12alpha-helices |
Halomonas halodenitrificans |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.7.2.5 |
nitric oxide reductase |
- |
Halomonas halodenitrificans |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.7.2.5 |
cytochrome c |
- |
Halomonas halodenitrificans |
|
1.7.2.5 |
heme |
subunit NorB contains a low-spin heme b center, a high-spin heme b3 center, and a non-heme FeB center |
Halomonas halodenitrificans |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
1.7.2.5 |
malfunction |
recombinant truncated NOR exhibits the same spectroscopic properties and reactivity to NO and O2 as wil-type NOR, although its enzymatic activity toward NO is considerably decreased |
Halomonas halodenitrificans |
1.7.2.5 |
additional information |
Halomonas halodenitrificans nitric oxide reductase (NOR) is the membrane-bound heterodimer complex of NorC, which contains a low-spin heme c center, and NorB, which contains a low-spin heme b center, a high-spin heme b3 center, and a non-heme FeB center |
Halomonas halodenitrificans |
1.7.2.5 |
physiological function |
NO reductase (NOR) protects denitrifying bacteria from NO, which is highly toxic, by converting it to N2O |
Halomonas halodenitrificans |