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Archives of Microbiology

, Volume 151, Issue 4, pp 307–313 | Cite as

Immunogold localization of coenzyme F420-reducing formate dehydrogenase and coenzyme F420-reducing hydrogenase in Methanobacterium formicicum

  • S. F. Baron
  • D. S. Williams
  • H. D. May
  • P. S. Patel
  • H. C. Aldrich
  • J. G. Ferry
Original Papers

Abstract

The ultrastructural locations of the coenzyme F420-reducing formate dehydrogenase and coenzyme F420-reducing hydrogenase of Methanobacterium formicicum were determined using immunogold labeling of thin-sectioned, Lowicryl-embedded cells. Both enzymes were located predominantly at the cell membrane. Whole cells displayed minimal F420-dependent formate dehydrogenase activity or F420-dependent hydrogenase activity, and little activity was released upon osmotic shock treatment, suggesting that these enzymes are not soluble periplasmic proteins. Analysis of the deduced amino acid sequences of the formate dehydrogenase subunits revealed no hydrophobic regions that could qualify as putative membrane-spanning domains.

Key words

Methanobacterium formicicum Formate dehydrogenase F420-hydrogenase Immunogold Ultrastructure Methanogen 

Abbreviation

PBST

Phosphate-buffered saline containing 0.1% (v/v) Triton X-100

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Copyright information

© Springer-Verlag 1989

Authors and Affiliations

  • S. F. Baron
    • 1
  • D. S. Williams
    • 2
  • H. D. May
    • 1
  • P. S. Patel
    • 1
  • H. C. Aldrich
    • 2
  • J. G. Ferry
    • 1
  1. 1.Department of Anaerobic MicrobiologyVirginia Polytechnic Institute and State UniversityBlacksburgUSA
  2. 2.Department of Microbiology and Cell SciencesUniversity of FloridaGainesvilleUSA

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