Ferrochelatase: Difference between revisions
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<StructureSection load='2qd2' size='450' side='right' scene=' | |||
<StructureSection load='2qd2' size='450' side='right' scene='' caption='Ferrochelatase with protoheme and Fe2S2 (PDB code [[2qd2]])'> | |||
'''Ferrochelatase''' (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster. Defective FECH is the cause of porphyria. | '''Ferrochelatase''' (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster. Defective FECH is the cause of porphyria. | ||
Revision as of 11:57, 11 December 2013
Ferrochelatase (FECH) catalyzes the last step in the formation of heme. FECH adds Fe+2 to protoporphyrin IX converting it to protoheme. The human FECH is a homodimer containing 2 similar domains and an iron-sulfur cluster. Defective FECH is the cause of porphyria. Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase [1] Ferrochelatase produces . It can also . However, the ability to insert other . In this way Bacillus subtilis ferrochelatase can insert copper into protoporphyrin IX, but to a much less extent cobalt. In contrast, the human and Saccharomyces cerevisiae ferrochelatases prefer cobalt over copper. shows that , while A third residue, Tyr in B. subtilis, is a third ligand via a water molecule. Human and S. cerevisiae ferrochelatase utilizes In the structures of the ferrochelatases the Tyr/Met occupies the same position. We also know that the Tyr residue of the is a . By site directed mutagenesis and showed that the metal specificity changed so that the modified B. subtilis ferrochelatase . Two crystal structures are presented. how . The how a in the B. subtilis enzyme. |
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3D structures of ferrochelatase3D structures of ferrochelatase
Updated on 11-December-2013
1ak1 – BsFECH – Bacillus subtilis
2ac4 - BsFECH (mutant)
1doz - BsFECH + Mg
1ld3 - BsFECH + Zn
2ac2 - BsFECH (mutant) + Zn
2h1v, 3goq - BsFECH (mutant) + Mg
2h1w - BsFECH (mutant) + Fe + Mg
2hk6 - BsFECH + Fe+ Mg
1n0i - BsFECH + Cd + Mg
3m4z - BsFECH + Co + Mg
1l8x - yFECH + Co – yeast
1lbq - yFECH
2qd4 - hFECH + Fe2S2 - human
1hrk, 2pnj, 2po5, 2po7, 3aqi, 4f4d - hFECH (mutant) + Fe2S2
Ferrochelatase complex with porphyrinFerrochelatase complex with porphyrin
2qd3, 3hcn, 3hco, 3hcp - hFECH + protoporphyrin IX + Fe2S2
3hcr - hFECH + protoporphyrin IX + O2 + Fe2S2
2hre, 2qd1, 2qd2 - hFECH (mutant) + protoporphyrin IX + Fe2S2
2qd5 - hFECH + protoporphyrin IX + Pb + Fe2S2
1c1h - BsFECH + N-methylmesoporphyrin + Mg
2q3j, 2q2o - BsFECH (mutant) + N-methylmesoporphyrin + Mg
2q2n – BsFECH + protoporphyrin IX + Mg
1c9e - BsFECH + N-methylmesoporphyrin + Cu + Mg
References
- ↑ Hansson MD, Karlberg T, Soderberg CA, Rajan S, Warren MJ, Al-Karadaghi S, Rigby SE, Hansson M. Bacterial ferrochelatase turns human: Tyr13 determines the apparent metal specificity of Bacillus subtilis ferrochelatase. J Biol Inorg Chem. 2010 Nov 4. PMID:21052751 doi:10.1007/s00775-010-0720-4