EC Number   |
Cofactor |
Reference |
|---|
    4.2.1.120 | 4Fe-4S-center |
- |
696521 |
| 4.2.1.120 | 4Fe-4S-center |
a [4Fe-4S]2+ cluster, coordinated by three cysteine and one histidine residues, is located 7 A from the Re-side of a flavin adenine dinucleotide moiety |
700926 |
| 4.2.1.120 | 4Fe-4S-center |
enzyme shows [4Fe-4S]2+ clusters, two clusters/homotetramer. The four iron atoms in each cluster are coordinated in an identical fashion, and there is no direct interaction with substrates. The Fe-S clusters serve a structural rather than a catalytic role in 4-hydroxybutyryl-CoA dehydratase |
697699 |
| 4.2.1.120 | 4Fe-4S-center |
Fe-S-cluster is difficult to reduce. No equilibration of electrons between the flavin and the Fe-S-center |
696186 |
| 4.2.1.120 | 4Fe-4S-center |
one 4Fe-4S-center per subunit |
695914 |
| 4.2.1.120 | FAD |
2 mol FAD per mol of enzyme |
2965 |
| 4.2.1.120 | FAD |
2 mol per mol of enzyme |
2966 |
| 4.2.1.120 | FAD |
a [4Fe-4S]2+cluster, coordinated by three cysteine and one histidine residues, is located 7 A from the Re-side of a flavin adenine dinucleotide moiety |
700926 |
| 4.2.1.120 | FAD |
one FAD per enzyme subunit, FAD contents of enzyme mutants compared to the wild-type, overview |
746825 |
| 4.2.1.120 | FAD |
protein-bound FAD, is easily reduced to the semiquinone and only slowly to the hydroquinone. No equilibration of electrons between the flavin and the Fe-S-center |
696186 |
