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Isoprenoid biosynthesis via the MEP pathway: in vivo Mössbauer spectroscopy identifies a [4Fe-4S]2+ center with unusual coordination sphere in the LytB protein.
J Am Chem Soc. 2009 Sep 23; 131(37):13184-5.JA

Abstract

The MEP pathway for the biosynthesis of isoprene units is present in most pathogenic bacteria, in the parasite responsible for malaria, and in plant plastids. This pathway is absent in animals and is accordingly a target for the development of antimicrobial drugs. LytB, also called IspH, the last enzyme of this pathway catalyzes the conversion of (E)-4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) using an oxygen sensitive iron sulfur cluster. The exact nature of this iron sulfur cluster is still a matter of debate. We have used (57)Fe Mössbauer spectroscopy to investigate the LytB cluster in whole E. coli cells and in the anaerobically purified enzyme: In LytB an unusual [4Fe-4S](2+) cluster is attached to the protein by three conserved cysteines and contains a hexacoordinated iron linked to three sulfurs of the cluster and three additional oxygen or nitrogen ligands.

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Publisher Full Text (DOI)

Authors+Show Affiliations

Seemann M
Université de Strasbourg, Institut de Chimie, UMR CNRS UDS 7177, 4 rue Blaise Pascal, 67070 Strasbourg, France. mseemann@chimie.u-strasbg.fr
Janthawornpong K
No affiliation info available
Schweizer J
No affiliation info available
Böttger LH
No affiliation info available
Janoschka A
No affiliation info available
Ahrens-Botzong A
No affiliation info available
Tambou EN
No affiliation info available
Rotthaus O
No affiliation info available
Trautwein AX
No affiliation info available
Rohmer M
No affiliation info available

MeSH

AnaerobiosisErythritolEscherichia coliEscherichia coli ProteinsIronOxidoreductasesSpectroscopy, MossbauerSugar PhosphatesSulfurTerpenes

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19708647

Citation

Seemann, Myriam, et al. "Isoprenoid Biosynthesis Via the MEP Pathway: in Vivo Mössbauer Spectroscopy Identifies a [4Fe-4S]2+ Center With Unusual Coordination Sphere in the LytB Protein." Journal of the American Chemical Society, vol. 131, no. 37, 2009, pp. 13184-5.
Seemann M, Janthawornpong K, Schweizer J, et al. Isoprenoid biosynthesis via the MEP pathway: in vivo Mössbauer spectroscopy identifies a [4Fe-4S]2+ center with unusual coordination sphere in the LytB protein. J Am Chem Soc. 2009;131(37):13184-5.
Seemann, M., Janthawornpong, K., Schweizer, J., Böttger, L. H., Janoschka, A., Ahrens-Botzong, A., Tambou, E. N., Rotthaus, O., Trautwein, A. X., & Rohmer, M. (2009). Isoprenoid biosynthesis via the MEP pathway: in vivo Mössbauer spectroscopy identifies a [4Fe-4S]2+ center with unusual coordination sphere in the LytB protein. Journal of the American Chemical Society, 131(37), 13184-5. https://doi.org/10.1021/ja9012408
Seemann M, et al. Isoprenoid Biosynthesis Via the MEP Pathway: in Vivo Mössbauer Spectroscopy Identifies a [4Fe-4S]2+ Center With Unusual Coordination Sphere in the LytB Protein. J Am Chem Soc. 2009 Sep 23;131(37):13184-5. PubMed PMID: 19708647.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Isoprenoid biosynthesis via the MEP pathway: in vivo Mössbauer spectroscopy identifies a [4Fe-4S]2+ center with unusual coordination sphere in the LytB protein. AU - Seemann,Myriam, AU - Janthawornpong,Karnjapan, AU - Schweizer,Julia, AU - Böttger,Lars H, AU - Janoschka,Adam, AU - Ahrens-Botzong,Anne, AU - Tambou,Erasmienne Ngouamegne, AU - Rotthaus,Olaf, AU - Trautwein,Alfred X, AU - Rohmer,Michel, PY - 2009/8/28/entrez PY - 2009/8/28/pubmed PY - 2010/1/6/medline SP - 13184 EP - 5 JF - Journal of the American Chemical Society JO - J Am Chem Soc VL - 131 IS - 37 N2 - The MEP pathway for the biosynthesis of isoprene units is present in most pathogenic bacteria, in the parasite responsible for malaria, and in plant plastids. This pathway is absent in animals and is accordingly a target for the development of antimicrobial drugs. LytB, also called IspH, the last enzyme of this pathway catalyzes the conversion of (E)-4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) using an oxygen sensitive iron sulfur cluster. The exact nature of this iron sulfur cluster is still a matter of debate. We have used (57)Fe Mössbauer spectroscopy to investigate the LytB cluster in whole E. coli cells and in the anaerobically purified enzyme: In LytB an unusual [4Fe-4S](2+) cluster is attached to the protein by three conserved cysteines and contains a hexacoordinated iron linked to three sulfurs of the cluster and three additional oxygen or nitrogen ligands. SN - 1520-5126 UR - https://www.unboundmedicine.com/medline/citation/19708647/Isoprenoid_biosynthesis_via_the_MEP_pathway:_in_vivo_M��ssbauer_spectroscopy_identifies_a_[4Fe_4S]2+_center_with_unusual_coordination_sphere_in_the_LytB_protein_ L2 - https://doi.org/10.1021/ja9012408 DB - PRIME DP - Unbound Medicine ER -