FAD requirement for the reduction of coenzyme F420 by hydrogenase from Methanobacterium formicicum

Michael J.K. Nelson, David P. Brown, James G. Ferry

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13 Scopus citations


Hydrophobic interaction chromatography of coenzyme F420-reducing hydrogenase purified from Methanobacterium formicicum depleted protein-bound FAD and eliminated the ability to reduce coenzyme F420. Preincubation of the FAD-depleted hydrogenase with FAD restored 85% of the coenzyme F420-reducing activity. FMN did not replace FAD. A Kd of 12 μM was estimated for FAD. Analysis of the reactivated hydrogenase following molecular sieve column chromatography showed that FAD was bound to protein. The results indicate that protein-bound FAD is reversibly removed from the coenzyme F420-reducing hydrogenase and that this flavin is required for the reduction of coenzyme F420.

Original languageEnglish (US)
Pages (from-to)775-781
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - May 16 1984

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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