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Literature summary extracted from
- The archaeal SoxABCD complex is a proton pump in Sulfolobus acidocaldarius (1997), J. Biol. Chem., 272, 8417-8426.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.4 | cyanide | 2 mM, oxidation of caldariella quinol and N,N,N',N'-tetramethyl-1,4-phenylenediamine is completely inhibited | Sulfolobus acidocaldarius |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.1.1.4 | 0.026 | - |
caldariellaquinol | pH 6.5, 50°C, enzyme in liposomes (tetraether lipids) | Sulfolobus acidocaldarius | |
| 7.1.1.4 | 0.036 | - |
caldariellaquinol | pH 6.5, 50°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside) | Sulfolobus acidocaldarius | |
| 7.1.1.4 | 0.046 | - |
N,N,N',N'-tetramethyl-1,4-phenylenediamine | pH 6.5, 40°C, enzyme in liposomes (tetraether lipids) | Sulfolobus acidocaldarius | |
| 7.1.1.4 | 0.067 | - |
N,N,N',N'-tetramethyl-1,4-phenylenediamine | pH 6.5, 40°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside) | Sulfolobus acidocaldarius | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.4 | copper | the enzyme contains one copper atom | Sulfolobus acidocaldarius | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 7.1.1.4 | 280000 | - |
gel filtration | Sulfolobus acidocaldarius |
| 7.1.1.4 | 570000 | - |
when membrane solubilization is carried out at low salt concentration, an oligomeric state of the oxidase is obtained | Sulfolobus acidocaldarius |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.1.1.4 | Sulfolobus acidocaldarius | P39480 and P98004 and P39479 and P39477 | P39480 (soxC) and P98004 (soxB) and P39479 (soxA) and P39477 (Saci_2086) | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.1.1.4 | - |
Sulfolobus acidocaldarius |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.4 | caldariellaquinol + O2 + n H+/in | the SoxABCD complex is a proton-pumping quinol oxidase. With N,N,N',N'-tetramethyl-1,4-phenylenediamine as a reductant, the SoxABCD complex reconstituted into liposomes generates a proton motive force. The purified SoxABCD oxidase does not react with cytochrome c or blue copper proteins such as halocyanine or azurine as electron donors. However, considerable turnover numbers are found with N,N,N',N'-tetramethyl-1,4-phenylenediamine or caldariella quinol, confirming that in vivo the enzyme is acting as a quinol oxidase | Sulfolobus acidocaldarius | caldariellaquinone + H2O + n H+/out | - |
? | |
| 7.1.1.4 | N,N,N',N'-tetramethyl-1,4-phenylenediamine + O2 + n H+/in | the SoxABCD complex is a proton-pumping quinol oxidase. With N,N,N',N'-tetramethyl-1,4-phenylenediamine as a reductant, the SoxABCD complex reconstituted into liposomes generates a proton motive force. The purified SoxABCD oxidase does not react with cytochrome c or blue copper proteins such as halocyanine or azurin as electron donors. However, considerable turnover numbers are found with N,N,N',N'-tetramethyl-1,4-phenylenediamine or caldariellaquinol, confirming that in vivo the enzyme is acting as a quinol oxidase | Sulfolobus acidocaldarius | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.1.1.4 | SoxABCD complex | - |
Sulfolobus acidocaldarius |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.1.1.4 | 157 | - |
N,N,N',N'-tetramethyl-1,4-phenylenediamine | pH 6.5, 40°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside) | Sulfolobus acidocaldarius | |
| 7.1.1.4 | 239 | - |
caldariellaquinol | pH 6.5, 50°C, enzyme in liposomes (tetraether lipids) | Sulfolobus acidocaldarius | |
| 7.1.1.4 | 393 | - |
caldariellaquinol | pH 6.5, 50°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside) | Sulfolobus acidocaldarius | |
| 7.1.1.4 | 404 | - |
N,N,N',N'-tetramethyl-1,4-phenylenediamine | pH 6.5, 40°C, enzyme in liposomes (tetraether lipids) | Sulfolobus acidocaldarius | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.4 | heme | the enzyme contains four heme a redox centers. The EPR spectra indicate the presence of three low spin and one high spin heme species, the latter associated with the binuclear heme CuB site. The standard midpoint potentials of the cytochrome a587 heme centers are +210 and +270 mV, respectively | Sulfolobus acidocaldarius | |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 7.1.1.4 | 2300 | - |
N,N,N',N'-tetramethyl-1,4-phenylenediamine | pH 6.5, 40°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside) | Sulfolobus acidocaldarius | |
| 7.1.1.4 | 8700 | - |
N,N,N',N'-tetramethyl-1,4-phenylenediamine | pH 6.5, 40°C, enzyme in liposomes (tetraether lipids) | Sulfolobus acidocaldarius | |
| 7.1.1.4 | 9200 | - |
caldariellaquinol | pH 6.5, 50°C, enzyme in liposomes (tetraether lipids) | Sulfolobus acidocaldarius | |
| 7.1.1.4 | 11000 | - |
caldariellaquinol | pH 6.5, 50°C, enzyme in detergent micelle (dodecyl-beta-D-maltoside) | Sulfolobus acidocaldarius | |
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