1.9.6.1	4Fe-4S-center	the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster	712967	
1.9.6.1	bis(molybdopterin guanine dinucleotide)molybdenum cofactor	NapA contains a molybdo-bis(molybdopterin guanine dinucleotide) cofactor	674891	
1.9.6.1	bis(molybdopterin guanine dinucleotide)molybdenum cofactor	subunit NapA is an 90000 Da catalytic subunit which binds a bis-molybdenum guanosine dinucleoside cofactor and a [4Fe4S] cluster	654561	
1.9.6.1	cytochrome	NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinone-ubiquinol couple via cytochrome NapC and NapB to NapA	696082	
1.9.6.1	cytochrome	presence of a bound cytochrome	395176	
1.9.6.1	cytochrome	the membrane-bound cytochrome NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB	700256	
1.9.6.1	cytochrome c	-	741478, 742319, 742645, 742648	
1.9.6.1	cytochrome c	di-heme cytochrome c redox partner, NapB	742486	
1.9.6.1	cytochrome c	i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB	742319	
1.9.6.1	cytochrome c	two surface-exposed c-type hemes, NapB	741958	
1.9.6.1	cytochrome c552	the enzyme is a complex of a 93000 Da polypeptide and a 16000 Da nitrate-oxidizable cytochrome c552, cytochrome c552 contains two c-type heme moieties	697696	
1.9.6.1	heme	a [4Fe-4S] cluster and two c-type hemes form an intramolecular electron transfer chain that deliver electrons to the active site. Residue lysine 56 connects, through hydrogen-bonds, the [4Fe-4S] center to one of the pyranopterin ligands of the Mo-cofactor	764214	
1.9.6.1	heme	contains 1.3 mol heme per mol of protein (assuminga 110-kDa molecular mass)	697696	
1.9.6.1	heme	subunit NapB is a diheme cytochrome c	697968	
1.9.6.1	heme	the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB)	674891	
1.9.6.1	molybdenum cofactor	-	699015, 741478, 742319, 742486	
1.9.6.1	molybdenum cofactor	a Mo-pyranopterin cofactor	742648	
1.9.6.1	molybdenum cofactor	i.e. MoCo, the EPR signature of the MoCo is heterogeneous. The MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation. The inactive form features an open, oxidized pyranopterin, which is closed upon reduction. Distict from that, a slow, reversible inactivation/reactivation process occurs at high nitrate concentration, overview	741958	
1.9.6.1	molybdenum cofactor	synthesis of the Mo-pyranopterin cofactor, overview	742319	
1.9.6.1	molybdopterin	the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor	712967	
1.9.6.1	additional information	enzyme contains no flavin	395176	
1.9.6.1	[4Fe-4S] cluster	-	742319, 742486	
1.9.6.1	[4Fe-4S] cluster	in close proximity to the MoCo	741958	
1.9.6.1	[4Fe-4S]-center	-	764685	
1.9.6.1	[4Fe-4S]-center	a [4Fe-4S] cluster and two c-type hemes form an intramolecular electron transfer chain that deliver electrons to the active site. Residue lysine 56 connects, through hydrogen-bonds, the [4Fe-4S] center to one of the pyranopterin ligands of the Mo-cofactor	764214