EC Number   |
Cofactor |
Reference |
|---|
    1.14.13.236 | FAD |
- |
740073 |
| 1.14.13.236 | Ferredoxin |
- |
740073 |
| 1.14.13.236 | Ferredoxin |
ferredoxin binding leads to rearrangement of a loop about 30 A distal with a tightly matched, hydrogen bonded contact surface that places the [2Fe-2S] and diiron centres in their closest possible approach for electron transfer |
741045 |
| 1.14.13.236 | iron-sulfur centre |
complexes with phenolic products yield an asymmetric my-phenoxo-bridged diiron center and a shift of diiron ligand E231 into a hydrogen bonding position with conserved residue T201 |
740052 |
| 1.14.13.236 | iron-sulfur centre |
component contains a Rieske ferredoxin centre. H-bonding to the Rieske [2Fe-2S] center involves four (H47, Q48, A66, and H67 of T4MOC) of the five backbone amide H-bonds expected, the fifth backbone amide (I50 of T4MOC) fails to exhibit a hyperfine shift |
740035 |
| 1.14.13.236 | iron-sulfur centre |
component T4MOC contains a Rieske-type iron-sulfur center |
740033 |
| 1.14.13.236 | iron-sulfur centre |
study of the Fe(II)Fe(II) active site in the hydroxylase component of toluene-4 monoxygenase and the complex of T4moH bound by its effector protein, T4moD. Binding of the effector protein changes the geometry of one iron center and orientation of its redox active orbital to accommodate the binding of O2 in a bridged structure for efficient 2-electron transfer that can form a peroxo intermediate |
704171 |
