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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 iona cationan inorganic cationa divalent inorganic cation
an ionan inorganic ionan inorganic cationa divalent inorganic cation

Component of:
ferrous sulfate heptahydrate
iron sulfate

Chemical Formula: Fe

Molecular Weight: 55.847 Daltons

Monoisotopic Molecular Weight: 55.9349421 Daltons

SMILES: [Fe++]

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


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

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

Reactions known to consume the compound:

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+
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:
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:

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

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

In Reactions of unknown directionality:

Not in pathways:
Fur + Fe2+ = Fur-Fe+2
Fur + Fe2+ = Fur-Fe+2

In Transport reactions:
Fe2+[cytosol] + H+[periplasm]Fe2+[periplasm] + H+[cytosol],
Fe2+[periplasm] + H+[periplasm]Fe2+[cytosol] + H+[cytosol],
an ion[periplasm]an ion[extracellular space]

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]

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 [Vogel74a], N-acetylornithine aminotransferase [Vogel74b], 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, 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

This compound has been characterized as an alternative cofactor or prosthetic group of the following enzymes: anthranilate synthase, phenylhydantoinase

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


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

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

Vogel74a: 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

Vogel74b: 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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