1.3.7.7	4Fe-4S-center	-	711198, 713102	
1.3.7.7	4Fe-4S-center	NB-protein of DPOR carries two oxygen-tolerant [4Fe–4S] clusters	686758	
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	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	ADP	-	393862, 672324, 686758, 700718, 711198, 712026, 712268, 713251, 713252	
1.3.7.7	ATP	-	713102, 725412, 726104, 726255, 726394, 726526	
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	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	
1.3.7.7	ATP	subunit L contains the ATP-binding motif	672764	
1.3.7.7	Ferredoxin	-	725412, 726104, 726255, 726394, 726526	
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	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	reaction potential of the Fe–S cluster shows pH-dependence	743401