TSRI's main web site PROMISE mirror at TSRI Metalloprotein DB site Created: 2 May 1996
Last modified: 3 February 1999


Iron-sulphur proteins

Iron-sulphur proteins can be classified according to their biological function, by Fe-S centre type, by type and number of prosthetic centres, and by sequence similarity.

Iron-sulphur proteins by function

Function Protein class / family
Catalysis Oxidoreductases
  • Bacterial nitrate reductase
  • Formate dehydrogenase
  • Fumarate reductase
  • Glutamine PRPP amidotransferase
  • Hydrogenase
  • Methane monooxygenase
  • NADH:ubiquinone reductase
  • Phthalate dioxygenase reductase
  • Succinate dehydrogenase
  • Sulphite reductase
  • Xanthine dehydrogenase
Hydro­lyases
  • Aconitase
Electron transfer
  • Ferredoxins
  • Rieske proteins
  • Rubredoxins
  • Iron-sulphur proteins by Fe-S centre type

    Iron-sulphur centre Protein class / family
    FeCys4 image
    Fe(SgammaCys)4
  • Fe(Cys)4 proteins
  • [Fe2S2] image
    [Fe2S2](SgammaCys)4
  • Fe2S2 proteins
  • Rieske image
    [Fe2S2](SgammaCys)2(NdeltaHis)2
    [Fe4S4]Cys4 image
    [Fe4S4](SgammaCys)4
  • Fe4S4 proteins
  • [Fe4S4]Cys3His(Ndelta) image
    [Fe4S4](SgammaCys)3NdeltaHis
    [Fe4S4]Cys3His(Nepsilon) image
    [Fe4S4](SgammaCys)3NepsilonHis
    [Fe4S4]Cys3COOH image
    [Fe4S4](SgammaCys)3OdeltaAsp
    [Fe4S4] image
    [Fe4S4](SgammaCys)3(H2O)n
    [Fe3S4] image
    [Fe3S4](SgammaCys)3
  • Fe3S4 proteins
  • Pox cluster image
    [Fe8S7](SgammaCys)6NCysOgammaSer
  • Mo­nitrogenase component I
  • Pn cluster image
    [Fe8S7](SgammaCys)6
    Fe4S3O2X image
    [Fe4S3O2X](SgammaCys)4(OepsilonGlu)2NepsilonHis
  • `Prismane' proteins (cluster II)
  • Some `extinct species' of iron-sulphur clusters (now shown to be erroneous)
    [Fe3S3] image
    [Fe3S3](SgammaCys)5OepsilonGlu
  • Fe3S3 iron-sulphur proteins - see Bacterial­type ferredoxins
      Erroneous modelling of the [Fe3S4] cluster
  • Fe8S8 cluster image
    [Fe8S8](SgammaCys)6OgammaSer
  • Mo­nitrogenase component I
      [Fe8S8] model for P­cluster was incorrectly proposed after modelling a single structure to a superposition of electron densities from a mixture of the two types of [Fe8S7] clusters
  • [Fe6S6] image
    [Fe6S6](L)6 (L=ligand)
  • Fe6S6 proteins - see `Prismane' proteins
      Proposed on the basis of the similarity of the EPR spectra to those of the synthetic compounds with [Fe6S6] core
  • Iron-sulphur proteins by type and number of prosthetic centres

    Iron-sulphur proteins
    Simple Complex

    Iron-sulphur proteins in motif databases

    PRINTS ID PRINTS AC PROSITE/BLOCKS ID PROSITE AC BLOCKS AC
    2FE2SFRDOXIN PR00159 2FE2S_FERREDOXIN PS00197 BL00197
    3FE4SFRDOXIN PR00352
    -
    -
    -
    4FE4SFRDOXIN PR00353 4FE4S_FERREDOXIN PS00198 BL00198
    7FE8SFRDOXIN PR00354
    ACONITASE PR00415 ACONITASE PS00450 BL00450
    ADRENODOXIN PR00355 ADX PS00814 BL00814
    -
    -
    ENDONUCLEASE_III_1
    ENDONUCLEASE_III_2
    PS00764
    PS01155
    BL00764
    -
    -
    GATASE_TYPE_II PS00443 BL00443
    HIPIPFRDOXIN PR00374 HIPIP PS00596 BL00596
    NIHGNASESMLL PR00614
    -
    -
    -
    -
    -
    NITROGENASE_1_1
    NITROGENASE_1_2
    PS00699
    PS00090
    BL00699
    NITROGNASEII PR00091 NIFH_FRXC_1
    NIFH_FRXC_2
    PS00746
    PS00692
    BL00746
    -
    -
    PUR_PYR_PR_TRANSFER PS00103 BL00103
    RIESKE PR00162 RIESKE_1
    RIESKE_2
    PS00199
    PS00200
    BL00199
    RNGDIOXGNASE PR00090 RING_HYDROXYL_ALPHA PS00570 BL00570
    RUBREDOXIN PR00163 RUBREDOXIN PS00202 BL00202
    SIROHAEM PR00397 NIR_SIR PS00365 BL00365

    Iron-sulphur proteins in PROMISE

    PROMISE ID Description
    ACONITASE Aconitases, iron­responsive element binding proteins (IRE­BP), and alpha­isopropylmalate isomerases
    ADRENODOXIN Adrenodoxin­type ferredoxins (including adrenodoxin, putidaredoxin and terpredoxin)
    ARHD Aromatic­ring­hydroxylating dioxygenases
    AOR Aldehyde ferredoxin oxidoreductase family
    BACFRDX Bacterial­type mono­, di­ and polycluster ferredoxins
    DESULFOREDOXIN Desulforedoxin­type Fe(Cys)4 proteins
    DFX Desulfoferrodoxin
    DMSOR DMSO reductase family
    ENDONUCLEASE3 Endonuclease III
    FEHASE Iron hydrogenases
    GPATASE Glutamine PRPP amidotransferase
    HIPIP High potential iron-sulphur proteins
    NIFE Nickel-iron hydrogenase
    NITROGENASE1 Mo­nitrogenase component I (MoFe protein)
    NITROGENASE2 Mo­nitrogenase component II (Fe protein)
    PLANTFRDX Plant­type ferredoxins
    PRISMANE `Prismane' proteins
    RIESKE Rieske iron-sulphur proteins
    RUBREDOXIN Rubredoxin­type Fe(Cys)4 proteins
    RUBRERYTHRIN Rubrerythrin
    SIROHAEM Sirohaem-Fe4S4 enzymes (including sulphite reductases and assimilatory nitrite reductases)
    TMADH Trimethylamine dehydrogenase
    XANTOXIDASE Xanthine oxidase family (including xanthine oxidase, xanthine dehydrogenase, aldehyde oxidase, CO dehydrogenase)

    HET groups in PDB (at BSM)

    HET group Description Formula HET group Description Formula
    FE
    Iron(III) ion Fe3+
    FE2
    Iron(II) ion Fe2+
    FES
    [Fe2S2] cluster Fe2S2
    F2S
    [Fe2S2] cluster Fe2S2
    F3S
    [Fe3S4] cluster Fe3S4
    F4S
    [Fe4S4] cluster Fe4S4
    FS3
    [Fe3S4] cluster Fe3S4
    FS4
    [Fe4S4] cluster Fe4S4
    CLF
    P­cluster of Mo­nitrogenase component I Fe8S7
    CLP*
    P­cluster of Mo­nitrogenase component I Fe8S8*
    ZN
    Zinc ion Zn2+

    * The [Fe8S8] cluster model appears to be wrong.

    Iron-sulphur proteins in 3­D databases

    Fe-S centre Electron­transfer proteins Enzymes
    Fe(Cys)4
  • Desulforedoxin
  • Rubredoxins
  • Rubrerythrin
  • -
    Fe2S2
  • Adrenodoxin­type ferredoxins
  • Plant­type ferredoxins
  • Rieske iron-sulphur proteins
  • Xanthine oxidase family
  • Fe4S4 / Fe3S4
  • Bacterial­type ferredoxins
  • HiPIPs
  • Aconitases
  • Aldehyde ferredoxin oxidoreductase
  • DMSO reductase family
  • Endonuclease III
  • Iron hydrogenases
  • Glutamine PRPP amidotransferase
  • Mo­nitrogenase component I
  • Mo­nitrogenase component II
  • Nickel-iron hydrogenase
  • Trimethylamine dehydrogenase
  • References

    1. Bertini, I., Ciurli, S. and Luchinat, C. (1995) The electronic structure of FeS centers in proteins and models. A contribution to the understanding of their electron transfer properties. Structure and Bonding 83, 1-53.
    2. Cowan, J.A. (1993) Inorganic Biochemistry: An Introduction. VCH Publishers, New York.
    3. IUPAC-IUB commission on biochemical nomenclature (CBN) (1973) Nomenclature of iron-sulfur proteins. 1973 recommendations. Eur. J. Biochem. 35, 1-2.
    4. Nomenclature Committee of the International Union of Biochemistry (NC-IUB) (1979) Nomenclature of iron-sulfur proteins. Recommendations 1978. Eur. J. Biochem. 93, 427-430.
    5. Nomenclature Committee of the International Union of Biochemistry (NC-IUB) (1991) Nomenclature of electron­transfer proteins. Recommendations 1989. Eur. J. Biochem. 200, 599-611.
    General references on iron-sulphur proteins