EC Number   |
Subunits |
Reference |
|---|
    1.1.2.3 | ? |
x * 45000, SDS-PAGE |
743494 |
| 1.1.2.3 | ? |
x * 47000, recombinantly expressed flavocytochrome b2 flavin-binding domain, SDS-PAGE |
696075 |
| 1.1.2.3 | homodimer |
2 * 68000, Na-DDS electrophoresis |
-, 762626 |
| 1.1.2.3 | homotetramer |
- |
-, 712523, 743420, 763745 |
| 1.1.2.3 | homotetramer |
4 * 57500, X-ray crystallography |
695890 |
| 1.1.2.3 | homotetramer |
each subunit of the soluble tetrameric enzyme consists of an N-terminal b5-like heme-binding domain and a C terminal flavodehydrogenase. The first 99 residues are folded around the heme, the next about 390 constitute the FMN-binding domain, and the last residues up to 511 make contacts with the other three subunits. Thus, the flavodehydrogenase domains constitute the core of the molecule, with a fourfold symmetry, while the heme domains lie at the periphery |
722153 |
| 1.1.2.3 | homotetramer |
enzyme-substrate structure analysis during thr reaction cycle, overview |
697905 |
| 1.1.2.3 | homotetramer |
the enzyme is a tetramer with four identical subunits, each consisting of FMN- and heme-binding domains |
-, 743847, 743862 |
| 1.1.2.3 | homotetramer |
x-ray crystallography |
712759 |
| 1.1.2.3 | tetramer |
- |
348074, 696302, 699506 |
