Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-decylchinolone | pI50: 4.9 | Sulfolobus acidocaldarius | |
2-dodecyl-N-hydroxychinolone | pI50: 5.9 | Sulfolobus acidocaldarius | |
2-methyl-3-dodecyl-N-hydroxy-chinolone | pI50: 7.3 | Sulfolobus acidocaldarius | |
2-methyl-3-dodecylchinolone | pI50: 6.2 | Sulfolobus acidocaldarius | |
3-methyl-2-decylchinolone | pI50: 5.5 | Sulfolobus acidocaldarius | |
cyanide | - |
Sulfolobus acidocaldarius | |
EDTA | causes maximal inhibition of either the isolated enzyme, or the activity of the crude membrane extract by 63% with a half-maximal effect at 21 mM | Sulfolobus acidocaldarius | |
additional information | benzoquinone, naphthoquinone and phenol derivatives do not influence the reactivity | Sulfolobus acidocaldarius | |
phosphate | inhibitory effect which at the pH-optimum and 50 mM phosphate concentration amounts to about 35% | Sulfolobus acidocaldarius |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.036 | - |
caldariellaquinol | pH 4.5, 50°C | Sulfolobus acidocaldarius | |
0.057 | - |
ferrocytochrome c | pH 4.5, 50°C | Sulfolobus acidocaldarius |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu | the enzyme contains a total of seven metal redox centers. One of it, the blue copper protein sulfocyanin, functionally links two subcomplexes. One is a bb3-type terminal oxidase moiety containing CuA and CuB, whereas the other consists of a Rieske FeS-protein and a homolog to cytochrome b – in this case hosting two hemes AS. Based on a 1:1 stoichiometry, 1 mol complex contains 6 mol Fe and 4 mol Cu | Sulfolobus acidocaldarius | |
Fe | the enzyme contains a total of seven metal redox centers. One of it, the blue copper protein sulfocyanin, functionally links two subcomplexes. One is a bb3-type terminal oxidase moiety containing CuA and CuB, whereas the other consists of a Rieske FeS-protein and a homolog to cytochrome b – in this case hosting two hemes AS. Based on a 1:1 stoichiometry, 1 mol complex contains 6 mol Fe and 4 mol Cu | Sulfolobus acidocaldarius |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
224000 | - |
gel filtration | Sulfolobus acidocaldarius |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
caldariellaquinol + O2 + n H+/in | Sulfolobus acidocaldarius | function as a redox-driven proton pump, within the SoxGFE assembly of the supercomplex acting as a caldariella-quinol:sulfocyanin oxidoreductase | caldariellaquinone + H2O + n H+/out | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sulfolobus acidocaldarius | P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768 | P39481 (soxM), Q97UN3 (soxG), Q53765 (soxE), Q53766 (soxD), Q59825 (soxH), Q53768 (soxI) | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4 ferrocytochrome c + O2 + 4 H+ | enzymatic activity is monitored with reduced cytochrome c despite not being the natural substrate. Sulfolobus acidocaldarius does not contain any c-type cytochrome. However, it can be used for in vitro assays of the terminal oxidase moiety in the complex because electrons can be accepted form either sulfocyanin (SoxE) or from SoxH. SoxABCD does not react with cytochrome c. The tested activity is specific for the SoxM complex | Sulfolobus acidocaldarius | 4 ferricytochrome c + 2 H2O | - |
? | |
caldariellaquinol + O2 + n H+/in | function as a redox-driven proton pump, within the SoxGFE assembly of the supercomplex acting as a caldariella-quinol:sulfocyanin oxidoreductase | Sulfolobus acidocaldarius | caldariellaquinone + H2O + n H+/out | - |
? | |
caldariellaquinol + O2 + n H+/in | the SoxM-complex can oxidize the electron donor horseheart cytochrome c as well as caldariellaquinol. Based on genetic information it is suggested that the complex provides two proton pumping sites. However a preparation of liposomes with tetraether lipids together with the complex is not sufficient to perform proton pumping experiments | Sulfolobus acidocaldarius | caldariellaquinone + H2O + n H+/out | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | 6 polypeptide subunits: SoxM (87000 Da), SoxG (56000 Da), SoxE (21000 Da) , SoxF (26800 Da), SoxH (16300 Da), SoxI (16800 Da). Proposed structural organization of the supercomplex: therein the polypeptides SoxG, SoxF, and SoxE represent an assembly. Sulfocyanin (SoxE) has a typical membrane spanning N-terminal anchor sequence fixing it firmly to the complex | Sulfolobus acidocaldarius |
Synonyms | Comment | Organism |
---|---|---|
SoxM supercomplex | - |
Sulfolobus acidocaldarius |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
assay at | Sulfolobus acidocaldarius |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4.5 | - |
assay at | Sulfolobus acidocaldarius |
5.3 | - |
- |
Sulfolobus acidocaldarius |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | the enzyme contains 2 heme As and 2 heme B (b and b3) | Sulfolobus acidocaldarius |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme may be involved in the electron pathway, it may be involved in regulatory adaptation to environmental stress | Sulfolobus acidocaldarius |