EC Number   |
Cofactor |
Reference  |
|---|
   1.3.7.7 | ADP |
- |
393862, 672324, 686758, 700718, 711198, 712026, 712268, 713251, 713252 |
| 1.3.7.7 | 4Fe-4S-center |
the enzyme contains an Fe-S cluster as redox center in all subunits |
672764 |
| 1.3.7.7 | ATP |
subunit L contains the ATP-binding motif |
672764 |
| 1.3.7.7 | 4Fe-4S-center |
NB-protein of DPOR carries two oxygen-tolerant [4Fe4S] clusters |
686758 |
| 1.3.7.7 | 4Fe-4S-center |
the L-protein carries a [4Fe-4S] cluster between the protomers that is very similar to that of the nitrogenase Fe protein. The NB-protein also carries a [4Fe-4S] cluster that mediates electrons from the L-cluster to the protochlorophyllide molecule |
712026 |
| 1.3.7.7 | ATP |
dependent on, the homodimeric ChlL2 bearing an intersubunit [4Fe-4S] cluster is an ATP-dependent reductase |
712465 |
| 1.3.7.7 | Ferredoxin |
the enzyme contains intersubunit [4Fe-4S] cluster in the homodimer formed by two ChlL subunits. The [4Fe-4S] cluster coordinated by an aspartate oxygen alongside three cysteine ligands, structure, overview. Iron-sulfur cluster coordination in DPOR compared to nitrogenase, overview |
712465 |
| 1.3.7.7 | 4Fe-4S-center |
- |
711198, 713102 |
| 1.3.7.7 | Ferredoxin |
each catalytic BchN-BchB unit contains one protochlorophyllidee and one iron-sulfur NB-cluster coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity, overview |
713102 |
| 1.3.7.7 | ATP |
dependent on, the homodimeric subunit ChlL2 functions as an ATP-dependent switch protein, triggering the transient interaction of ChlL2 and heterotetrameric catalytic subunit (ChlN/ChlB)2 |
725877 |
