2.0 2012-07-30 14:55:20 -0600 2015-06-03 17:21:10 -0600 ECMDB21332 M2MDB001733 ferroxamine minus Fe(3) Ferrioxamine is catalyzed by fhuF. The phenotype of fhuF mutants and the structural features of the FhuF protein suggest that FhuF is involved in the reduction of ferric iron in cytoplasmic ferrioxamine B. (PMID 9990318) Insertional inactivation and gene replacement of both genes showed that while FhuD2 is involved in the transport of iron(III) in complex with ferrichrome, ferrioxamine B, aerobactin, and coprogen, FhuD1 shows a more limited substrate range, capable of only iron(III)-ferrichrome and iron(III)-ferrioxamine B transport in S. (PMID 11489851) Removal of iron from coprogen, ferrichrome, and ferrioxamine B was significantly lower in fhuF mutants compared to the corresponding parental strains, which suggested that FhuF is involved in iron removal from these hydroxamate-type siderophores. (PMID 14756576) N-5-4-5-acetyl(hydroxy)aminopentylamino-4-oxobutanoyl-hydroxyaminopentyl-N'-(5-aminopentyl)-N'-hydroxybutanediamide; iron(3+) C25H48FeN6O8 616.529 616.288304675 iron(3+) ion 3-[(5-aminopentyl)(hydroxy)carbamoyl]-N-[5-(N-hydroxy-3-{[5-(N-hydroxyacetamido)pentyl]-C-hydroxycarbonimidoyl}propanamido)pentyl]propanimidic acid iron(3+) ion deferoxamine [Fe+3].CC(=O)N(O)CCCCCN=C(O)CCC(=O)N(O)CCCCCN=C(O)CCC(=O)N(O)CCCCCN InChI=1S/C25H48N6O8.Fe/c1-21(32)29(37)18-9-3-6-16-27-22(33)12-14-25(36)31(39)20-10-4-7-17-28-23(34)11-13-24(35)30(38)19-8-2-5-15-26;/h37-39H,2-20,26H2,1H3,(H,27,33)(H,28,34);/q;+3 BLMKUGGNEDBRRA-UHFFFAOYSA-N Cytosol Extra-organism Periplasm logp -2.6 ChemAxon pka_strongest_acidic 7 ChemAxon pka_strongest_basic 10.23 ChemAxon iupac iron(3+) ion 3-[(5-aminopentyl)(hydroxy)carbamoyl]-N-[5-(N-hydroxy-3-{[5-(N-hydroxyacetamido)pentyl]-C-hydroxycarbonimidoyl}propanamido)pentyl]propanimidic acid ChemAxon average_mass 616.529 ChemAxon mono_mass 616.288304675 ChemAxon smiles [Fe+3].CC(=O)N(O)CCCCCN=C(O)CCC(=O)N(O)CCCCCN=C(O)CCC(=O)N(O)CCCCCN ChemAxon formula C25H48FeN6O8 ChemAxon inchi InChI=1S/C25H48N6O8.Fe/c1-21(32)29(37)18-9-3-6-16-27-22(33)12-14-25(36)31(39)20-10-4-7-17-28-23(34)11-13-24(35)30(38)19-8-2-5-15-26;/h37-39H,2-20,26H2,1H3,(H,27,33)(H,28,34);/q;+3 ChemAxon inchikey BLMKUGGNEDBRRA-UHFFFAOYSA-N ChemAxon polar_surface_area 212.82 ChemAxon refractivity 145.99 ChemAxon polarizability 63.42 ChemAxon rotatable_bond_count 23 ChemAxon acceptor_count 11 ChemAxon donor_count 6 ChemAxon physiological_charge 1 ChemAxon formal_charge 3 ChemAxon Specdb::CMs 1083267 441292 Matzanke, B. F., Anemuller, S., Schunemann, V., Trautwein, A. X., Hantke, K. (2004). "FhuF, part of a siderophore-reductase system." Biochemistry 43:1386-1392. 14756576 Sebulsky, M. T., Heinrichs, D. E. (2001). "Identification and characterization of fhuD1 and fhuD2, two genes involved in iron-hydroxamate uptake in Staphylococcus aureus." J Bacteriol 183:4994-5000. 11489851 Ferric iron reductase protein fhuF P39405 FHUF_ECOLI fhuF http://ecmdb.ca/proteins/P39405.xml FADH2 + 2 Ferroxamine > FAD +2 Iron +2 ferroxamine minus Fe(3) +2 Hydrogen ion 2 Ferroxamine + FMNH >2 Iron +2 ferroxamine minus Fe(3) + Flavin Mononucleotide +2 Hydrogen ion 2 Ferroxamine + Reduced riboflavin >2 Iron +2 ferroxamine minus Fe(3) +2 Hydrogen ion + Riboflavin Fe3+ + ferroxamine minus Fe(3) > Ferroxamine