1.13.12.19	Fe2+	at the active site, enzyme acts as a bidentate ligand and it forms a complex with Fe2+. The Fe2+ is further coordinated to a tridentate Schiff base of 2-oxoglutarate and L-arginine, whose terminal carboxylate and guanidino groups are trapped by binding sites I and II on the enzyme, respectively	714008	
1.13.12.19	Fe2+	dependent on, required for catalysis	741936, 742153	
1.13.12.19	Fe2+	dependent on, required for catalysis. The overall metal-binding mode of PsEFE is relatively typical for 2OG oxygenases, with the metal coordinated by His189 (C terminus of DSBH II), Asp191 (loop linking DSBH II and III), and His268 (N-terminus of DSBH VII)	743692	
1.13.12.19	Fe2+	dependent on, residues H189, D191 and H268 are responsible for binding the Fe(II) ligand	744563	
1.13.12.19	Fe2+	Fe2+-dependent enzyme	764978, 765536	
1.13.12.19	Fe2+	non-heme Fe(II)-dependent ethylene-forming enzyme, the metal ion is hexa-coordinated	742750	
1.13.12.19	Fe2+	required, KM value 0.059 mM	715784	
1.13.12.19	Fe2+	the nonheme iron(II) oxygenase catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinate and CO2 to generate a highly reactive iron species that hydroxylates a specific alkane C-H bond, in this case targeting L-arginine (Arg) for hydroxylation	764156