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Escherichia coli K-12 substr. MG1655 Compound: Fe2+

Synonyms: Fe+2, Fe++, ferrous iron, Fe+2, ferrous ion, fe(ii)

Superclasses: an ion a cation

Component of:
ferrous sulfate heptahydrate
iron sulfate
Fur-Fe+2

Chemical Formula: Fe

Molecular Weight: 55.847 Daltons

Monoisotopic Molecular Weight: 55.9349421 Daltons

SMILES: [Fe++]

InChI: InChI=1S/Fe/q+2

InChIKey: InChIKey=CWYNVVGOOAEACU-UHFFFAOYSA-N

Unification Links: ChEBI:29033 , ChemSpider:25394 , HMDB:HMDB00692 , IAF1260:33552 , KEGG:C14818 , MetaboLights:MTBLC29033 , PubChem:27284

Standard Gibbs Free Energy of Change Formation (ΔfG in kcal/mol): -18.85

Reactions known to consume the compound:

heme biosynthesis I (aerobic) , heme biosynthesis II (anaerobic) , superpathway of heme biosynthesis from uroporphyrinogen-III :
Fe2+ + protoporphyrin IX → protoheme IX + 2 H+

Not in pathways:
hydrogen peroxide + Fe2+ → hydroxyl radical + Fe3+ + OH-
2 Fe2+ + 2 oxygen → 2 superoxide + 2 Fe3+
4 Fe2+ + 4 H+ + oxygen → 4 Fe3+ + 2 H2O

Reactions known to produce the compound:

Not in pathways:
protoheme IX + 2 H+ → protoporphyrin IX + Fe2+
2 Fe2+ + 2 a siderophore + NADP+ + H+ ← 2 an Fe(III)-siderophore + NADPH
2 Fe2+ + 2 (2,3-dihydroxybenzoylserine)3 + NADP+ ← 2 ferric (2,3-dihydroxybenzoylserine)3 + NADPH + 9 H+

Reactions known to both consume and produce the compound:

siroheme biosynthesis :
sirohydrochlorin + Fe2+ ↔ siroheme + 2 H+

In Reactions of unknown directionality:

Not in pathways:
4 Fe2+ + oxygen + 6 H2O = 4 [FeO(OH)] monomer + 8 H+
2 Fe2+ + oxygen + 4 H2O = 2 [FeO(OH)] monomer + hydrogen peroxide + 4 H+
2 Fe2+ + hydrogen peroxide + 2 H2O = 2 [FeO(OH)] monomer + 4 H+
Fur + Fe2+ = Fur-Fe+2

In Transport reactions:
Fe2+[periplasmic space]Fe2+[cytosol] ,
Fe2+[cytosol] + H+[periplasmic space]Fe2+[periplasmic space] + H+[cytosol] ,
Fe2+[periplasmic space] + H+[periplasmic space]Fe2+[cytosol] + H+[cytosol]

Enzymes activated by Fe2+, sorted by the type of activation, are:

Activator (Mechanism unknown) of: adenosylmethionine decarboxylase [Lu07] , 2-dehydro-3-deoxyphosphoheptonate aldolase [Ray91] , dimethyl sulfoxide reductase [Weiner88] , D-mannonate dehydratase [RobertBaudouy73, Dreyer87] , D-altronate dehydratase [RobertBaudouy82, Smiley60, Dreyer87] , trimethylamine N-oxide reductase [Sagai73]

Enzymes inhibited by Fe2+, sorted by the type of inhibition, are:

Inhibitor (Mechanism unknown) of: N-acetyl-β-neuraminate lyase [Aisaka91, Comment 1] , NADPH-dependent curcumin reductase [Hassaninasab11] , ribonucleoside-triphosphate reductase [Eliasson92] , deoxyribose 1,5-phosphomutase [HammerJespersen70] , N-acetylglutamylphosphate reductase [Vogel74] , acetylornithine aminotransferase [Vogel74a] , N-acetylneuraminate lyase [Aisaka91, Comment 1] , phosphoglucomutase [Joshi64] , o-succinylbenzoate-CoA ligase [Kwon96] , D-aminopropanol dehydrogenase [Kelley84]

This compound has been characterized as a cofactor or prosthetic group of the following enzymes: protein-arginine oxygenase , catalase , adenine deaminase , threonine dehydrogenase , ribonucleoside-diphosphate reductase , hydrogenase , formate dehydrogenase , ribulose-5-phosphate 3-epimerase , cAMP phosphodiesterase , UDP-glucose:α-D-galactose-1-phosphate uridylyltransferase , L-1,2-propanediol oxidoreductase , glycolaldehyde reductase , L-glutamate:NADP+ oxidoreductase (transaminating) , galactarate dehydratase , 1-ethyladenine demethylase , N1-methyladenine demethylase , N3-methylcytosine demethylase , 3-(2,3-dihydroxyphenyl)propionate 1,2-dioxygenase , acetaldehyde dehydrogenase , cytosine deaminase , 2-dehydro-3-deoxyphosphoheptonate aldolase , pyruvate formate-lyase deactivase , acyl carrier protein phosphodiesterase , alcohol dehydrogenase , peptide deformylase , methionine aminopeptidase , taurine dioxygenase

In Growth Media: MOPS medium with 2% glycerol , M63 medium with 2% glycerol , MOPS medium with 2% glucose , MOPS medium with 0.4% glucose , MOPS medium base , Neidhardt EZ rich defined medium , trace metal solution , M63 medium with 2% glucose , LB enriched , ATCC medium 57 , M56 medium , M63 medium base


References

Aisaka91: Aisaka K, Igarashi A, Yamaguchi K, Uwajima T (1991). "Purification, crystallization and characterization of N-acetylneuraminate lyase from Escherichia coli." Biochem J 1991;276 ( Pt 2);541-6. PMID: 1646603

Dreyer87: Dreyer JL (1987). "The role of iron in the activation of mannonic and altronic acid hydratases, two Fe-requiring hydro-lyases." Eur J Biochem 166(3);623-30. PMID: 3038546

Eliasson92: Eliasson R, Pontis E, Fontecave M, Gerez C, Harder J, Jornvall H, Krook M, Reichard P (1992). "Characterization of components of the anaerobic ribonucleotide reductase system from Escherichia coli." J Biol Chem 267(35);25541-7. PMID: 1460049

HammerJespersen70: Hammer-Jespersen K, Munch-Petersen A (1970). "Phosphodeoxyribomutase from Escherichia coli. Purification and some properties." Eur J Biochem 1970;17(3);397-407. PMID: 4992818

Hassaninasab11: Hassaninasab A, Hashimoto Y, Tomita-Yokotani K, Kobayashi M (2011). "Discovery of the curcumin metabolic pathway involving a unique enzyme in an intestinal microorganism." Proc Natl Acad Sci U S A 108(16):6615-20. PMID: 21467222

Joshi64: Joshi JG, Handler P (1964). "Phosphoglucomutase. I. Purification and properties of phosphoglucomutase from Escherichia coli." J. Biol. Chem. 239:2741-2751. PMID: 14216423

Kelley84: Kelley JJ, Dekker EE (1984). "D-1-amino-2-propanol:NAD+ oxidoreductase. Purification and general properties of the large molecular form of the enzyme from Escherichia coli K12." J Biol Chem 1984;259(4);2124-9. PMID: 6365902

Kwon96: Kwon O, Bhattacharyya DK, Meganathan R (1996). "Menaquinone (vitamin K2) biosynthesis: overexpression, purification, and properties of o-succinylbenzoyl-coenzyme A synthetase from Escherichia coli." J Bacteriol 1996;178(23);6778-81. PMID: 8955296

Lu07: Lu ZJ, Markham GD (2007). "Metal ion activation of S-adenosylmethionine decarboxylase reflects cation charge density." Biochemistry 46(27);8172-80. PMID: 17567041

Ray91: Ray JM, Bauerle R (1991). "Purification and properties of tryptophan-sensitive 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli." J Bacteriol 173(6);1894-901. PMID: 1672127

RobertBaudouy73: Robert-Baudouy JM, Stoeber FR (1973). "[Purification and properties of D-mannonate hydrolyase from Escherichia coli K12]." Biochim Biophys Acta 1973;309(2);473-85. PMID: 4581499

RobertBaudouy82: Robert-Baudouy J, Jimeno-Abendano J, Stoeber F (1982). "D-Mannonate and D-altronate dehydratases of Escherichia coli K12." Methods Enzymol 1982;90 Pt E;288-94. PMID: 6759855

Sagai73: Sagai M, Ishimoto M (1973). "An enzyme reducing adenosine 1N-oxide in Escherichia coli, amine N-oxide reductase." J Biochem (Tokyo) 1973;73(4);843-59. PMID: 4578389

Smiley60: Smiley JD, Ashwell G (1960). "Uronic acid metabolism in bacteria. III. Purification and properties of D-altronic acid and D-mannonic acid dehydrases in Escherichia coli." J Biol Chem 235;1571-5. PMID: 13831814

Vogel74: Vogel HJ, Vogel RH (1974). "Enzymes of arginine biosynthesis and their repressive control." Adv Enzymol Relat Areas Mol Biol 1974;40(0);65-90. PMID: 4365537

Vogel74a: Vogel, HJ, Vogel, RH "Enzymes of Arginine Biosynthesis." Advances in Enzymology, 40:70 (1974).

Weiner88: Weiner JH, MacIsaac DP, Bishop RE, Bilous PT (1988). "Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity." J Bacteriol 1988;170(4);1505-10. PMID: 3280546


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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