Mitochondrial ferritin

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Mitochondrial ferritin is a ferroxidase enzyme that in humans is encoded by the FTMT gene.[1]

It is classified as a metal-binding protein which is located within the mitochondria. After the protein is taken up by the mitochondria it can be processed into a mature protein and assemble functional ferritin shells.

## Structure

Its structure was determined at 1.70 Å through the use of X-ray diffraction and contains 182 residues. It is 67% helical. The Ramachandran plot shows that the structure of mitochondrial ferritin is mainly alpha helical with a low prevalence of beta sheets.

## References

1. ↑ "A human mitochondrial ferritin encoded by an intronless gene". J. Biol. Chem. 276 (27): 24437–40. July 2001. doi:10.1074/jbc.C100141200. PMID 11323407.

## Further reading

* "Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala.". J. Mol. Biol. 340 (2): 277–93. 2004. doi:10.1016/j.jmb.2004.04.036. PMID 15201052.
* "The effects of frataxin silencing in HeLa cells are rescued by the expression of human mitochondrial ferritin.". Biochim. Biophys. Acta 1782 (2): 90–8. 2008. doi:10.1016/j.bbadis.2007.11.006. PMID 18160053. https://hal.archives-ouvertes.fr/hal-00501557/file/PEER_stage2_10.1016%2Fj.bbadis.2007.11.006.pdf.
* "Tissue-specific expression of ferritin H regulates cellular iron homoeostasis in vivo.". Biochem. J. 395 (3): 501–7. 2006. doi:10.1042/BJ20060063. PMID 16448386.
* "Hemin-mediated regulation of an antioxidant-responsive element of the human ferritin H gene and role of Ref-1 during erythroid differentiation of K562 cells.". Mol. Cell. Biol. 26 (7): 2845–56. 2006. doi:10.1128/MCB.26.7.2845-2856.2006. PMID 16537925.
* "Ferritin contains less iron (59Fe) in cells when the protein pores are unfolded by mutation.". J. Biol. Chem. 283 (46): 31394–400. 2008. doi:10.1074/jbc.M806025200. PMID 18805796.
* "Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia.". Blood 101 (5): 1996–2000. 2003. doi:10.1182/blood-2002-07-2006. PMID 12406866.
* "Detection and functional analysis of an SNP in the promoter of the human ferritin H gene that modulates the gene expression.". Gene 377: 1–5. 2006. doi:10.1016/j.gene.2006.02.034. PMID 16797877.
* "PIAS3 interacts with ATF1 and regulates the human ferritin H gene through an antioxidant-responsive element.". J. Biol. Chem. 282 (31): 22335–43. 2007. doi:10.1074/jbc.M701477200. PMID 17565989.
* "Elevated intracellular calcium increases ferritin H expression through an NFAT-independent post-transcriptional mechanism involving mRNA stabilization.". Biochem. J. 411 (1): 107–13. 2008. doi:10.1042/BJ20071544. PMID 18076382.
* "Mitochondrial ferritin: a new player in iron metabolism.". Blood Cells Mol. Dis. 29 (3): 376–83. 2002. doi:10.1006/bcmd.2002.0577. PMID 12547228.
* "Ferritin: a novel mechanism for delivery of iron to the brain and other organs.". Am. J. Physiol., Cell Physiol. 293 (2): C641–9. 2007. doi:10.1152/ajpcell.00599.2006. PMID 17459943.
* "Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: hypothesis for a protective role in Friedreich ataxia.". Hum. Mol. Genet. 18 (1): 1–11. 2009. doi:10.1093/hmg/ddn308. PMID 18815198.
* "The putative "nucleation site" in human H-chain ferritin is not required for mineralization of the iron core.". Biochemistry 43 (14): 4332–7. 2004. doi:10.1021/bi0498813. PMID 15065877.
* "Computational modeling of the dizinc-ferroxidase complex of human H ferritin: direct comparison of the density functional theory calculated and experimental structures.". J. Biol. Inorg. Chem. 14 (8): 1199–208. 2009. doi:10.1007/s00775-009-0563-z. PMID 19585161.
* "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
* "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2002. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
* "Role and regulation of ferritin H in rotenone-mediated mitochondrial oxidative stress.". Free Radic. Biol. Med. 44 (9): 1762–71. 2008. doi:10.1016/j.freeradbiomed.2008.01.031. PMID 18325346.
* "Unique iron binding and oxidation properties of human mitochondrial ferritin: a comparative analysis with Human H-chain ferritin.". J. Mol. Biol. 347 (3): 543–54. 2005. doi:10.1016/j.jmb.2005.01.007. PMID 15755449.
* "p53-mediated downregulation of H ferritin promoter transcriptional efficiency via NF-Y.". Int. J. Biochem. Cell Biol. 40 (10): 2110–9. 2008. doi:10.1016/j.biocel.2008.02.010. PMID 18372207.
* "Mitochondrial ferritin in the substantia nigra in restless legs syndrome.". J. Neuropathol. Exp. Neurol. 68 (11): 1193–9. 2009. doi:10.1097/NEN.0b013e3181bdc44f. PMID 19816198.

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Other oxidoreductases (EC 1.15-1.21)

1.15: Acting on superoxide as acceptor|

* Superoxide dismutase
* SOD1
* SOD2
* SOD3

1.16: Oxidizing metal ions|

* Ceruloplasmin

1.17: Acting on CH or CH2 groups|

* Xanthine oxidase
* Ribonucleotide reductase
* 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase

1.18: Acting on iron-sulfur proteins as donors|

* Nitrogenase

1.19: Acting on reduced flavodoxin as donor|

* Nitrogenase (flavodoxin)

1.20: Acting on phosphorus or arsenic in donors|

* Glutaredoxin
* GLRX
* GLRX2
* GLRX3
* GLRX5

1.21: Acting on X-H and Y-H to form an X-Y bond|

* Isopenicillin N synthase
* Columbamine oxidase
* Reticuline oxidase
* Sulochrin oxidase
* (+)-bisdechlorogeodin-forming
* (-)-bisdechlorogeodin-forming
* Aureusidin synthase
* Tetrahydrocannabinolic acid synthase
* Cannabidiolic acid synthase
* Dichlorochromopyrrolate synthase

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Enzymes

Activity|

* Active site
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* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Catalytically perfect enzyme
* Coenzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
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* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
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* EC1 Oxidoreductases (list)
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