1.9.6.1	Fe	contains 2.7 mol iron (of which 1.4 mol is presumably non-haem iron) per mol of protein (assuming a 110000 Da molecular mass)	697696	
1.9.6.1	Fe	NapA contains a [4Fe-4S] cluster	674891	
1.9.6.1	Fe	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	Fe2+	-	741478	
1.9.6.1	Fe2+	in the cofactor heme and the [4Fe-4S] cluster	742486	
1.9.6.1	Fe2+	in the heme/cytochrome cofactor	742319, 742648	
1.9.6.1	Iron	contains iron	395176	
1.9.6.1	Iron	Fe:Mo ratio is slightly higher than the theoretical value of 4:1	764685	
1.9.6.1	Iron	relative metal content is around 1 Mo atom to 6 Fe atoms	764214	
1.9.6.1	Mo	contains molybdenum, 0.9 mol molybdenum: 1 mol protein (assuminga 110000 Da molecular mass)	697696	
1.9.6.1	Mo	molybdoprotein	697968	
1.9.6.1	Mo	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	Mo(VI)	-	742319	
1.9.6.1	Mo(VI)	coordinates a cysteine and a sulfido residue	741478, 742319, 742648	
1.9.6.1	Mo5+	NapA contains a molybdo-bis(molybdopterin guanine dinucleotide) cofactor. The molybdenum ion coordination sphere of NapA includes two molybdopterin guanine dinucleotide dithiolenes, a protein-derived cysteinyl ligand and an oxygen atom. The Mo-O bond length is 2.6 A, which is indicative of a water ligand. In NapA or NapAB, the Mo5+ state can not be further reduced to Mo4+. A catalytic cycle for NapA is proposed in which nitrate binds to the Mo5+ ion and where a stable des-oxo Mo6+ species may participate	674891	
1.9.6.1	Mo6+	NapA contains a molybdo-bis(molybdopterin guanine dinucleotide) cofactor. The molybdenum ion coordination sphere of NapA includes two molybdopterin guanine dinucleotide dithiolenes, a protein-derived cysteinyl ligand and an oxygen atom. The Mo-O bond length is 2.6 A, which is indicative of a water ligand. In NapA or NapAB, the Mo5+ state can not be further reduced to Mo4+. A catalytic cycle for NapA is proposed in which nitrate binds to the Mo5+ ion and where a stable des-oxo Mo6+ species may participate	674891	
1.9.6.1	Molybdenum	-	741478	
1.9.6.1	Molybdenum	92% Mo incorporation in active CNapA. The Fe:Mo ratio is slightly higher than the theoretical value of 4:1	764685	
1.9.6.1	Molybdenum	in the molybdenum cofactor. Role for NapD in the insertion of the molybdenum cofactor	742486	
1.9.6.1	Molybdenum	molybdenum-containing enzyme, the nitrate molecule binds to the active site with the molabdenum ion in the +6 oxidation state, electron transfer to the active site occurs only in the proton-electron transfer stage, where the molybdenum-V species plays an important role in catalysis	699199	
1.9.6.1	Molybdenum	the active site is a Mo bis-(pyranopterin guanine dinucleotide), relative metal content is around 1 Mo atom to 6 Fe atoms	764214	
1.9.6.1	Molybdenum	within the molybdenum cofactor. The coordination sphere of the Mo ion consists of the four thiolate ligands of two pyranopterins, a sulfur atom from a cysteine that attaches the MoCo to the protein backbone, and a sixth inorganic ligand, proposed to be oxygen or more recently sulfur	741958