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Identification
YMDB IDYMDB00379
NameIron(2+)
SpeciesSaccharomyces cerevisiae
StrainBaker's yeast
DescriptionIron(2+), also called ferrous iron, is iron in the +2 oxidation state. In animals, plants, and fungi, iron is often the metal ion incorporated into the heme complex. Heme is an essential component of cytochrome proteins, which mediate redox reactions, and of oxygen carrier proteins such as hemoglobin, myoglobin, and leghemoglobin. Inorganic iron also contributes to redox reactions in the iron-sulfur clusters of many enzymes, such as nitrogenase (involved in the synthesis of ammonia from nitrogen and hydrogen) and hydrogenase. Non-heme iron proteins include the enzymes methane monooxygenase (oxidizes methane to methanol), ribonucleotide reductase (reduces ribose to deoxyribose; DNA biosynthesis), hemerythrins (oxygen transport and fixation in Marine invertebrates) and purple acid phosphatase (hydrolysis of phosphate esters). [Wikipedia]
Structure
Thumb
Synonyms
  • FE (II) ION
  • Fe(2+)
  • Fe(II)
  • Fe2+
  • Ferrous ion
  • iron ion(2+)
  • Iron(2+)
  • Armco iron
  • Carbonyl iron
  • FE
  • Ferrovac e
  • Hematite
  • Infed
  • Limonite
  • LOHA
  • Magnetite
  • Malleable iron
  • Metopirone
  • Metyrapone
  • PZH2m
  • PZHO
  • Remko
  • Suy-b 2
  • Taconite
  • Venofer
  • Wrought iron
  • Iron hydroxide (fe(OH)3)
  • Iron oxyhydroxide
  • Ferric hydroxide
  • Iron hydroxide (III)
CAS number15438-31-0
WeightAverage: 55.845
Monoisotopic: 55.934942133
InChI KeyCWYNVVGOOAEACU-UHFFFAOYSA-N
InChIInChI=1S/Fe/q+2
IUPAC Namelambda2-iron(2+) ion
Traditional IUPAC Namelambda2-iron(2+) ion
Chemical FormulaFe
SMILES[Fe++]
Chemical Taxonomy
Description belongs to the class of inorganic compounds known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom.
KingdomInorganic compounds
Super ClassHomogeneous metal compounds
ClassHomogeneous transition metal compounds
Sub ClassNot Available
Direct ParentHomogeneous transition metal compounds
Alternative ParentsNot Available
Substituents
  • Homogeneous transition metal
Molecular FrameworkNot Available
External Descriptors
Physical Properties
StateNot Available
Charge2
Melting pointNot Available
Experimental Properties
PropertyValueReference
Water SolubilityNot AvailablePhysProp
LogPNot AvailablePhysProp
Predicted Properties
PropertyValueSource
logP-0.77ChemAxon
pKa (Strongest Acidic)4.58ChemAxon
Physiological Charge2ChemAxon
Hydrogen Acceptor Count0ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area0 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity0 m³·mol⁻¹ChemAxon
Polarizability1.78 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • extracellular
  • mitochondrion
  • cytoplasm
Organoleptic PropertiesNot Available
SMPDB Pathways
Porphyrin MetabolismPW002462 ThumbThumb?image type=greyscaleThumb?image type=simple
Pyrimidine metabolismPW002469 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Porphyrin and chlorophyll metabolismec00860 Map00860
Pyrimidine metabolismec00240 Map00240
SMPDB Reactions
Iron(2+) + Hydrogen + oxygenIron(3+) + water
Protoporphyrin IX + Iron(2+)Heme + Hydrogen
Heme + AH2 + oxygenBiliverdin + Iron(2+) + Carbon monoxide + A + water
KEGG Reactions
Iron(2+) + Protoporphyrin IXHeme + hydron
Sirohydrochlorin + Iron(2+)hydron + Siroheme
Concentrations
Intracellular ConcentrationsNot Available
Extracellular Concentrations
Intracellular ConcentrationSubstrateGrowth ConditionsStrainCitation
4 ± 1 µM hops, malted barleyanaerobicBaker's yeastAlcoholic beverage, wine, table, red - U.S. Department of Agriculture, Agricultural Research Service. 2010. USDA National Nutrient Database for Standard Reference, Release 23. Nutrient Data Laboratory Home Page
82 ± 0 µM grape juiceanaerobicBaker's yeastAlcoholic beverage, wine, table, red - U.S. Department of Agriculture, Agricultural Research Service. 2010. USDA National Nutrient Database for Standard Reference, Release 23. Nutrient Data Laboratory Home Page
Conversion Details Here
Spectra
Spectra
Spectrum TypeDescriptionSplash KeyView
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0a4i-9000000000-af3e7aec4f5bd9668683JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-0a4i-9000000000-af3e7aec4f5bd9668683JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-0a4i-9000000000-af3e7aec4f5bd9668683JSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-0udi-9000000000-3335fec4c3184739b75eJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-0udi-9000000000-3335fec4c3184739b75eJSpectraViewer
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-0udi-9000000000-3335fec4c3184739b75eJSpectraViewer
References
References:
  • UniProt Consortium (2011). "Ongoing and future developments at the Universal Protein Resource." Nucleic Acids Res 39:D214-D219.21051339
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Alcoholic beverage, wine, table, red - U.S. Department of Agriculture, Agricultural Research Service. 2010. USDA National Nutrient Database for Standard Reference, Release 23. Nutrient Data Laboratory Home Page
  • Schubert, H. L., Raux, E., Brindley, A. A., Leech, H. K., Wilson, K. S., Hill, C. P., Warren, M. J. (2002). "The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase." EMBO J 21:2068-2075.11980703
Synthesis Reference:Not Available
External Links:
ResourceLink
CHEBI ID29033
HMDB IDHMDB0000692
Pubchem Compound ID27284
Kegg IDC14818
ChemSpider ID25946211
FOODB IDFDB016251
WikipediaFerrous
BioCyc IDFE+2

Enzymes

General function:
Involved in ferrochelatase activity
Specific function:
Catalyzes the ferrous insertion into protoporphyrin IX
Gene Name:
HEM15
Uniprot ID:
P16622
Molecular weight:
44595.80078
Reactions
Protoheme + 2 H(+) → protoporphyrin + Fe(2+).
General function:
Involved in iron ion binding
Specific function:
Required for the uptake of Fe(3+) ions. May participate in the transport of electrons from cytoplasm to an extracellular substrate (Fe(3+) ion) via FAD and heme intermediates. Involved in iron homeostasis
Gene Name:
FRE8
Uniprot ID:
Q12209
Molecular weight:
78947.70313
Reactions
2 Fe(2+) + NAD(+) → 2 Fe(3+) + NADH.
General function:
Involved in binding
Specific function:
Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin- 2 into sirohydrochlorin and its subsequent ferrochelation into siroheme
Gene Name:
MET8
Uniprot ID:
P15807
Molecular weight:
31917.40039
Reactions
Precorrin-2 + NAD(+) → sirohydrochlorin + NADH.
Siroheme + 2 H(+) → sirohydrochlorin + Fe(2+).
General function:
Involved in oxidoreductase activity
Specific function:
Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane. Also participates in Cu(2+) reduction and Cu(+) uptake
Gene Name:
FRE1
Uniprot ID:
P32791
Molecular weight:
78853.0
Reactions
2 Fe(2+) + NADP(+) → 2 Fe(3+) + NADPH.
General function:
Involved in oxidoreductase activity
Specific function:
Siderophore-iron reductase responsible for reducing extracellular iron prior to import. Catalyzes the reductive uptake of Fe(3+) bound to dihydroxamate rhodotorulic acid. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane
Gene Name:
FRE4
Uniprot ID:
P53746
Molecular weight:
82014.60156
Reactions
2 Fe(2+) + NADP(+) → 2 Fe(3+) + NADPH.
General function:
Involved in oxidoreductase activity
Specific function:
Siderophore-iron reductase responsible for reducing extracellular iron prior to import. Catalyzes the reductive uptake of Fe(3+) bound to di- and trihydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane
Gene Name:
FRE3
Uniprot ID:
Q08905
Molecular weight:
80588.5
Reactions
2 Fe(2+) + NADP(+) → 2 Fe(3+) + NADPH.
General function:
Involved in ferroxidase activity
Specific function:
Promotes the biosynthesis of heme as well as the assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. Plays a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+). Can store large amounts of the metal in the form of a ferrihydrite mineral by oligomerization. May be involved in regulation of the mitochondrial electron transport chain
Gene Name:
YFH1
Uniprot ID:
Q07540
Molecular weight:
19490.0
Reactions
4 Fe(2+) + 4 H(+) + O(2) → 4 Fe(3+) + 2 H(2)O.
General function:
Involved in oxidoreductase activity
Specific function:
Cell surface metalloreductase
Gene Name:
FRE5
Uniprot ID:
Q08908
Molecular weight:
80291.70313
Reactions
2 Fe(2+) + NADP(+) → 2 Fe(3+) + NADPH.
General function:
Involved in oxidoreductase activity
Specific function:
Metalloreductase responsible for reducing vacuolar iron and copper prior to transport into the cytosol. Catalyzes the reduction of Fe(3+) to Fe(2+) and Cu(2+) to Cu(+), respectively, which can then be transported by the respective vacuolar efflux systems to the cytosol
Gene Name:
FRE6
Uniprot ID:
Q12473
Molecular weight:
81988.29688
Reactions
2 Fe(2+) + NADP(+) → 2 Fe(3+) + NADPH.
General function:
Involved in oxidoreductase activity
Specific function:
Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane. Also participates in Cu(2+) reduction and Cu(+) uptake
Gene Name:
FRE2
Uniprot ID:
P36033
Molecular weight:
80071.5
Reactions
2 Fe(2+) + NADP(+) → 2 Fe(3+) + NADPH.
General function:
Involved in oxidoreductase activity
Specific function:
Cell surface metalloreductase. May be involved in copper homeostasis
Gene Name:
FRE7
Uniprot ID:
Q12333
Molecular weight:
70904.70313
Reactions
2 Fe(2+) + NADP(+) → 2 Fe(3+) + NADPH.

Transporters

General function:
Involved in transmembrane transport
Specific function:
Required for Fe(2+) ion low affinity uptake
Gene Name:
FET4
Uniprot ID:
P40988
Molecular weight:
62791.5