, Volume 11, Issue 1, pp 159–168 | Cite as

Towards determining details of anaerobic growth coupled to ferric iron reduction by the acidophilic archaeon ‘Ferroplasma acidarmanus’ Fer1

  • Mark Dopson
  • Craig Baker-Austin
  • Philip BondEmail author
Original Paper


Elucidation of the different growth states of Ferroplasma species is crucial in understanding the cycling of iron in acid leaching sites. Therefore, a proteomic and biochemical study of anaerobic growth in ‘Ferroplasma acidarmanus’ Fer1 has been carried out. Anaerobic growth in Ferroplasma spp. occurred by coupling oxidation of organic carbon with the reduction of Fe3+; but sulfate, nitrate, sulfite, thiosulfate, and arsenate were not utilized as electron acceptors. Rates of Fe3+ reduction were similar to other acidophilic chemoorganotrophs. Analysis of the ‘F. acidarmanus’ Fer1 proteome by 2-dimensional polyacrylamide gel electrophoresis revealed ten key proteins linked with central metabolic pathways ≥4 fold up-regulated during anaerobic growth. These included proteins putatively identified as associated with the reductive tricarboxylic acid pathway used for anaerobic energy production, and others including a putative flavoprotein involved in electron transport. Inhibition of anaerobic growth and Fe3+ reduction by inhibitors suggests the involvement of electron transport in Fe3+ reduction. This study has increased the knowledge of anaerobic growth in this biotechnologically and environmentally important acidophilic archaeon.


Ferroplasma Proteomics Anaerobic Electron transport Metabolism 



Acid mine drainage


Elemental sulfur


Reduced inorganic sulfur compound


Mineral salts medium


2-Dimensional polyacrylamide gel electrophoresis


Matrix-assisted laser desorption ionization time-of-flight


1-Dimensional polyacrylamide gel electrophoresis


Tricarboxylic acid


2-Heptyl-4-Hydroxyquinoline N-oxide



We thank JF Banfield and KJ Edwards for provision of ‘F. acidarmanus’ Fer1 and helpful discussions. DJ Richardson is acknowledged for assistance in interpreting electron transport data. Trypsin digests and MALDI-TOF analysis of excised proteins was carried out at the John Innes Centre, Norwich. The technical assistance of M Maidment and L Flegg was greatly appreciated and R Evans-Gowing is acknowledged for taking the electron micrographs. This work was funded by a BBSRC Research grant.


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Copyright information

© Springer 2006

Authors and Affiliations

  • Mark Dopson
    • 1
    • 2
  • Craig Baker-Austin
    • 1
    • 5
  • Philip Bond
    • 1
    • 3
    • 4
    Email author
  1. 1.School of Biological SciencesUniversity of East AngliaNorwichUK
  2. 2.Molecular BiologyUmeå UniversityUmeaSweden
  3. 3.Centre for Ecology, Evolution and ConservationUniversity of East AngliaNorwichUK
  4. 4.Advanced Wastewater Management CentreUniversity of QueenslandQueenslandAustralia
  5. 5.Savannah River Ecology LaboratoryUniversity of GeorgiaAikenUSA

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