EC Number   |
Subunits |
Reference |
|---|
   7.1.1.4 | ? |
composed of at least five different subunits of 64900 Da, 38000 Da, 20400 Da, 18800 Da, and 7200 Da. Their genes are located in two different operons. While from both gene loci, a total of six genes are transcribed into mRNA, the pattern of polypeptides found in oxidase preparations comprises only four prominent protein bands on SDS-gels. The bands of 45000 Da, 40000 Da, 28000 Da, and 20000 Da can be assigned to proteins with calculated molecular masses of 38000 (DoxC), 64900 (DoxB), 18800 (DoxA), and 20400 (DoxD) Da, consistent with the frequent observation that membrane proteins display abnormal migration behavior upon denaturating SDS-PAGE. DoxB represents the catalytic core of the oxidase, exhibiting the typical consensus sequences for the heme- and copper-binding sites. Subunits doxA and doxB later classified as EC 1.8.5.2, thiosulfate dehydrogenase (quinone) |
-, 719689 |
| 7.1.1.4 | ? |
the doxD and doxA genes form a bicistronic operon in the Acidianus ambivalens genome, physically separated from the doxBCEF operon encoding the catalytic and the other subunits of the terminal quinol:oxygen oxidoreductase. Subunits with apparent molecular masses of 56000 Da (DoxB) and 61000 Da (DoxC) appear in the preparation of the terminal oxidase. Both enzymes 1. thiosulfate dehydrogenase (quinone) (EC 1.8.5.2, composed of the subunits DoxA and DoxD) and 2. caldariella quinol:dioxygen oxidoreductase (composed of the major subunits DoxB and DoxC and the minor subunit DoxE) form separate entities. The thiosulfate dehydrogenase (quinone) and the terminal oxidase might still form a loose aggregation in the membrane, transferring electrons rapidly either directly via the bound caldariella quinol molecule or indirectly via free caldariella quinol |
656833 |
| 7.1.1.4 | ? |
x * 18900 (SoxA) + x * 58000 (SoxB) + x * 62600 (SoxC) + SoxD + ?. The SoxABCD quinol oxidase complex contains at least five different polypeptides. In addition to the major subunits SoxA, SoxB and SoxC, it has two small polypeptides. One of these is the translation product of a short open reading frame (called the soxD gene) at the end of the operon |
720484 |
| 7.1.1.4 | ? |
x * 38000 |
-, 396010 |
| 7.1.1.4 | ? |
x * 40000 + x * 27000 + x * 20000, SDS-PAGE |
719514 |
| 7.1.1.4 | ? |
x * 47000 + x * 19000 + x * 11000, the enzyme is composed of at least three polypeptides, SDS-PAGE |
718705 |
| 7.1.1.4 | ? |
x * 87082, calulated from sequence |
719394 |
| 7.1.1.4 | 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 |
719024 |
| 7.1.1.4 | More |
SoxE is a constituent of the SoxM terminal oxidase supercomplex whereas SoxH, the CuA containing subunit II, escapes from the membrane fraction during preparation |
724988 |
| 7.1.1.4 | More |
SoxM is the core component of a second terminal oxidase complex. It forms a complex with at least SoxC and a 30 kDa Rieske Fe-S protein, but neither with SoxA nor SoxB |
719394 |
