Iron (ECMDB00692) (M2MDB000172)
Record Information | |||||||||||||||||||||||||||||||||||||||||||||||||
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Version | 2.0 | ||||||||||||||||||||||||||||||||||||||||||||||||
Creation Date | 2012-05-31 13:00:23 -0600 | ||||||||||||||||||||||||||||||||||||||||||||||||
Update Date | 2015-09-13 12:56:08 -0600 | ||||||||||||||||||||||||||||||||||||||||||||||||
Secondary Accession Numbers |
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Identification | |||||||||||||||||||||||||||||||||||||||||||||||||
Name: | Iron | ||||||||||||||||||||||||||||||||||||||||||||||||
Description | Iron is a chemical element with the symbol Fe and atomic number 26. Iron makes up 5% of the Earth's crust and is second in abundance to aluminium among the metals and fourth in abundance among the elements. Iron (as Fe2+, ferrous ion) is a necessary trace element used by all known living organisms. Iron-containing enzymes, usually containing heme prosthetic groups, participate in catalysis of oxidation reactions in biology, and in transport of a number of soluble gases. Its chief functions are in the transport of oxygen to tissue (hemoglobin) and in cellular oxidation mechanisms. Inorganic iron involved in redox reactions is also found in the iron-sulfur clusters of many enzymes, such as nitrogenase (involved in the synthesis of ammonia from nitrogen and hydrogen) and hydrogenase. A class of non-heme iron proteins is responsible for a wide range of functions such as ribonucleotide reductase (reduces ribose to deoxyribose; DNA biosynthesis) and purple acid phosphatase (hydrolysis of phosphate esters). When the body is fighting a bacterial infection, the body sequesters iron inside of cells (mostly stored in the storage molecule ferritin) so that it cannot be used by bacteria. Iron may promote both growth of E. coli. (PMID: 16151163) | ||||||||||||||||||||||||||||||||||||||||||||||||
Structure | |||||||||||||||||||||||||||||||||||||||||||||||||
Synonyms: |
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Chemical Formula: | Fe | ||||||||||||||||||||||||||||||||||||||||||||||||
Weight: | Average: 55.845 Monoisotopic: 55.934942133 | ||||||||||||||||||||||||||||||||||||||||||||||||
InChI Key: | CWYNVVGOOAEACU-UHFFFAOYSA-N | ||||||||||||||||||||||||||||||||||||||||||||||||
InChI: | InChI=1S/Fe/q+2 | ||||||||||||||||||||||||||||||||||||||||||||||||
CAS number: | 7439-89-6 | ||||||||||||||||||||||||||||||||||||||||||||||||
IUPAC Name: | lambda2-iron(2+) ion | ||||||||||||||||||||||||||||||||||||||||||||||||
Traditional IUPAC Name: | lambda2-iron(2+) ion | ||||||||||||||||||||||||||||||||||||||||||||||||
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. | ||||||||||||||||||||||||||||||||||||||||||||||||
Kingdom | Inorganic compounds | ||||||||||||||||||||||||||||||||||||||||||||||||
Super Class | Homogeneous metal compounds | ||||||||||||||||||||||||||||||||||||||||||||||||
Class | Homogeneous transition metal compounds | ||||||||||||||||||||||||||||||||||||||||||||||||
Sub Class | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
Direct Parent | Homogeneous transition metal compounds | ||||||||||||||||||||||||||||||||||||||||||||||||
Alternative Parents | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
Substituents |
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Molecular Framework | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
External Descriptors |
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Physical Properties | |||||||||||||||||||||||||||||||||||||||||||||||||
State: | Solid | ||||||||||||||||||||||||||||||||||||||||||||||||
Charge: | 2 | ||||||||||||||||||||||||||||||||||||||||||||||||
Melting point: | 1538 °C | ||||||||||||||||||||||||||||||||||||||||||||||||
Experimental Properties: |
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Predicted Properties |
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Biological Properties | |||||||||||||||||||||||||||||||||||||||||||||||||
Cellular Locations: | Cytoplasm | ||||||||||||||||||||||||||||||||||||||||||||||||
Reactions: | Adenosine triphosphate + FADH2 + 2 Iron + Water + SufBCD scaffold complex + 2 SufSE with bound sulfur > ADP + FAD +7 Hydrogen ion + Phosphate + SufBCD with bound [2Fe-2S] cluster +2 SufSE sulfur acceptor complex Adenosine triphosphate + FADH2 + 2 Iron + Water + SufBCD with bound [2Fe-2S] cluster + 2 SufSE with bound sulfur > ADP + FAD +7 Hydrogen ion + Phosphate + SufBCD with two bound [2Fe-2S] clusters +2 SufSE sulfur acceptor complex FADH2 + 2 Iron + 2 IscS with bound sulfur + IscU scaffold protein > FAD +6 Hydrogen ion +2 IscS sulfur acceptor protein + IscU with bound [2Fe-2S] cluster FADH2 + 2 Iron + 2 IscS with bound sulfur + IscU with bound [2Fe-2S] cluster > FAD +6 Hydrogen ion +2 IscS sulfur acceptor protein + IscU with two bound [2Fe-2S] clusters 4 Iron + 4 Hydrogen ion + Oxygen >4 Fe3+ +2 Water Iron + Protoporphyrin IX >2 Hydrogen ion + Heme [4Fe-4S] iron-sulfur cluster + 2 S-Adenosylmethionine + Hydrogen ion + NAD + octanoate (protein bound) > [2Fe-2S] iron-sulfur cluster +2 5'-Deoxyadenosine +2 Iron + lipoate (protein bound) +2 L-Methionine + NADH Iron + Sirohydrochlorin >3 Hydrogen ion + Siroheme Adenosine triphosphate + Water + Iron > ADP + Iron + Hydrogen ion + Phosphate Adenosine triphosphate + Water + Iron > ADP + Iron + Hydrogen ion + Phosphate FADH2 + 2 Fe3+ > FAD +2 Iron +2 Hydrogen ion [3Fe-4S] damaged iron-sulfur cluster + Iron > [4Fe-4S] iron-sulfur cluster 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 Hydrogen ion + Hydrogen peroxide + Iron > hydroxyl radical + OH<SUP>-</SUP> + Fe<SUP>3+</SUP> Oxygen + Iron > Superoxide anion + Fe<SUP>3+</SUP> Hydrogen ion + Heme Protoporphyrin IX + Iron Iron + Protoporphyrin IX > Heme + Hydrogen ion Iron + Hydrogen ion + Oxygen > Fe<SUP>3+</SUP> + Water Iron + a siderophore + NADP < an Fe(III)-siderophore + NADPH + Hydrogen ion Iron + (2,3-dihydroxybenzoylserine)<sub>3</sub> + NADP < ferric 2,3-dihydroxybenzoylserine + NADPH + Hydrogen ion Sirohydrochlorin + Iron <> Hydrogen ion + Siroheme Siroheme + 2 Hydrogen ion > Sirohydrochlorin + Iron 2 Iron + Hydrogen peroxide + 2 Hydrogen ion >2 Fe3+ +2 Water Heme + 2 Hydrogen ion > Protoporphyrin IX + Iron More...2 Iron + 2 an apo-siderophore + NADP + Hydrogen ion >2 an Fe(III)-siderophore + NADPH Protoporphyrin IX + Iron >2 Hydrogen ion + ferroheme b Sirohydrochlorin + Iron >2 Hydrogen ion + Siroheme | ||||||||||||||||||||||||||||||||||||||||||||||||
SMPDB Pathways: |
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KEGG Pathways: | |||||||||||||||||||||||||||||||||||||||||||||||||
EcoCyc Pathways: | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
Concentrations | |||||||||||||||||||||||||||||||||||||||||||||||||
Find out more about how we convert literature concentrations. | |||||||||||||||||||||||||||||||||||||||||||||||||
Spectra | |||||||||||||||||||||||||||||||||||||||||||||||||
Spectra: |
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References | |||||||||||||||||||||||||||||||||||||||||||||||||
References: |
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Synthesis Reference: | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||
Material Safety Data Sheet (MSDS) | Download (PDF) | ||||||||||||||||||||||||||||||||||||||||||||||||
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External Links: |
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Enzymes
- General function:
- Involved in metabolic process
- Specific function:
- Catalyzes the removal of elemental sulfur and selenium atoms from cysteine and selenocysteine to produce alanine. Functions as a sulfur delivery protein for NAD, biotin and Fe-S cluster synthesis. Transfers sulfur on 'Cys-456' of thiI in a transpersulfidation reaction. Transfers sulfur on 'Cys-19' of tusA in a transpersulfidation reaction. Functions also as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate
- Gene Name:
- iscS
- Uniprot ID:
- P0A6B7
- Molecular weight:
- 45089
Reactions
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. |
- General function:
- Involved in methyltransferase activity
- Specific function:
- Multifunctional enzyme that catalyzes the SAM-dependent methylation of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 and then position C-12 or C-18 to form trimethylpyrrocorphin 2. It also catalyzes the conversion of precorrin-2 into siroheme. This reaction consists of the NAD- dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme
- Gene Name:
- cysG
- Uniprot ID:
- P0AEA8
- Molecular weight:
- 49951
Reactions
S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. |
S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. |
Precorrin-2 + NAD(+) = sirohydrochlorin + NADH. |
Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+). |
- General function:
- Involved in oxidoreductase activity
- Specific function:
- Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides. Seems to reduces the complexed Fe(3+) iron of siderophores to Fe(2+), thus releasing it from the chelator
- Gene Name:
- fre
- Uniprot ID:
- P0AEN1
- Molecular weight:
- 26242
Reactions
Reduced riboflavin + NAD(P)(+) = riboflavin + NAD(P)H. |
2 cob(II)alamin + NAD(+) = 2 aquacob(III)alamin + NADH. |
- General function:
- Involved in ferrochelatase activity
- Specific function:
- Catalyzes the ferrous insertion into protoporphyrin IX
- Gene Name:
- hemH
- Uniprot ID:
- P23871
- Molecular weight:
- 35884
Reactions
Protoheme + 2 H(+) = protoporphyrin + Fe(2+). |
- General function:
- Involved in oxidoreductase activity
- Specific function:
- Probably involved in periplasmic detoxification of copper by oxidizing Cu(+) to Cu(2+) and thus preventing its uptake into the cytoplasm. Possesses phenoloxidase and ferroxidase activities and might be involved in the production of polyphenolic compounds and the prevention of oxidative damage in the periplasm
- Gene Name:
- cueO
- Uniprot ID:
- P36649
- Molecular weight:
- 56556
- General function:
- Involved in 2 iron, 2 sulfur cluster binding
- Specific function:
- Involved in the reduction of ferric iron in cytoplasmic ferrioxamine B
- Gene Name:
- fhuF
- Uniprot ID:
- P39405
- Molecular weight:
- 30113
- General function:
- Involved in catalytic activity
- Specific function:
- Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. Free octanoate is not a substrate for lipA
- Gene Name:
- lipA
- Uniprot ID:
- P60716
- Molecular weight:
- 36071
Reactions
Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine. |
- General function:
- Involved in metabolic process
- Specific function:
- Cysteine desulfurases mobilize the sulfur from L- cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo
- Gene Name:
- sufS
- Uniprot ID:
- P77444
- Molecular weight:
- 44433
Reactions
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. |
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor. |
- General function:
- Involved in nucleotide binding
- Specific function:
- Has low ATPase activity. The sufBCD complex acts synergistically with sufE to stimulate the cysteine desulfurase activity of sufS. The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation
- Gene Name:
- sufC
- Uniprot ID:
- P77499
- Molecular weight:
- 27582
- General function:
- Involved in GTP binding
- Specific function:
- GTP-driven Fe(2+) uptake system
- Gene Name:
- feoB
- Uniprot ID:
- P33650
- Molecular weight:
- 84473
- General function:
- Involved in iron-sulfur cluster assembly
- Specific function:
- The sufBCD complex acts synergistically with sufE to stimulate the cysteine desulfurase activity of sufS. The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation
- Gene Name:
- sufB
- Uniprot ID:
- P77522
- Molecular weight:
- 54745
- General function:
- Inorganic ion transport and metabolism
- Specific function:
- Specific function unknown
- Gene Name:
- cyaY
- Uniprot ID:
- P27838
- Molecular weight:
- 12231
- General function:
- Involved in iron ion binding
- Specific function:
- May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins (Potential)
- Gene Name:
- nifU
- Uniprot ID:
- P0ACD4
- Molecular weight:
- 13848
- General function:
- Not Available
- Specific function:
- Participates in cysteine desulfuration mediated by sufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for sufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of sufS, an intermediate product of cysteine desulfuration process. Together with the sufBCD complex, it thereby enhances up to 50- fold, the cysteine desulfurase activity of sufS. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Does not affect the selenocysteine lyase activity of sufS
- Gene Name:
- sufE
- Uniprot ID:
- P76194
- Molecular weight:
- 15800
- General function:
- Involved in iron-sulfur cluster assembly
- Specific function:
- The sufBCD complex acts synergistically with sufE to stimulate the cysteine desulfurase activity of sufS. The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the fhuF protein
- Gene Name:
- sufD
- Uniprot ID:
- P77689
- Molecular weight:
- 46822
- General function:
- Involved in response to stress
- Specific function:
- Involved in anaerobic NO protection
- Gene Name:
- ytfE
- Uniprot ID:
- P69506
- Molecular weight:
- 24882
- General function:
- Not Available
- Specific function:
- Not Available
- Gene Name:
- ftnA
- Uniprot ID:
- P0A998
- Molecular weight:
- Not Available
- General function:
- Inorganic ion transport and metabolism
- Specific function:
- May perform analogous functions in iron detoxification and storage to that of animal ferritins
- Gene Name:
- bfr
- Uniprot ID:
- P0ABD3
- Molecular weight:
- 18495
Reactions
4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. |
- General function:
- Inorganic ion transport and metabolism
- Specific function:
- Not Available
- Gene Name:
- yqjH
- Uniprot ID:
- Q46871
- Molecular weight:
- 28871
Reactions
2 Fe(II) + 2 an apo-siderophore + NADP(+) + H(+) = 2 an Fe(III)-siderophore + NADPH. |
Transporters
- General function:
- Involved in nucleotide binding
- Specific function:
- Has low ATPase activity. The sufBCD complex acts synergistically with sufE to stimulate the cysteine desulfurase activity of sufS. The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation
- Gene Name:
- sufC
- Uniprot ID:
- P77499
- Molecular weight:
- 27582
- General function:
- Involved in metal ion transmembrane transporter activity
- Specific function:
- Mediates zinc uptake. May also transport other divalent cations such as copper and cadmium ions
- Gene Name:
- zupT
- Uniprot ID:
- P0A8H3
- Molecular weight:
- 26484
- General function:
- Involved in transmembrane transport
- Specific function:
- Functions only as an uptake system for Fe(2+) ion acquisition
- Gene Name:
- efeU
- Uniprot ID:
- P75901
- Molecular weight:
- 30238
- General function:
- Involved in GTP binding
- Specific function:
- GTP-driven Fe(2+) uptake system
- Gene Name:
- feoB
- Uniprot ID:
- P33650
- Molecular weight:
- 84473
- General function:
- Involved in transporter activity
- Specific function:
- H(+)-stimulated, highly selective, manganese uptake system. Can also transport cadmium, cobalt, iron, zinc and to a lesser extent nickel and copper. Involved in response to reactive oxygen
- Gene Name:
- mntH
- Uniprot ID:
- P0A769
- Molecular weight:
- 44193
- General function:
- Involved in transporter activity
- Specific function:
- Non-specific porin
- Gene Name:
- ompN
- Uniprot ID:
- P77747
- Molecular weight:
- 41220
- General function:
- Involved in cation transmembrane transporter activity
- Specific function:
- Iron-efflux transporter responsible for iron detoxification. Also able to transport Zn(2+) in a proton- dependent manner
- Gene Name:
- fieF
- Uniprot ID:
- P69380
- Molecular weight:
- 32927
- General function:
- Involved in transporter activity
- Specific function:
- Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes
- Gene Name:
- phoE
- Uniprot ID:
- P02932
- Molecular weight:
- 38922
- General function:
- Involved in transporter activity
- Specific function:
- OmpF is a porin that forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane. It is also a receptor for the bacteriophage T2
- Gene Name:
- ompF
- Uniprot ID:
- P02931
- Molecular weight:
- 39333
- General function:
- Involved in transporter activity
- Specific function:
- Forms passive diffusion pores which allow small molecular weight hydrophilic materials across the outer membrane
- Gene Name:
- ompC
- Uniprot ID:
- P06996
- Molecular weight:
- 40368