Molybdenum and tungsten-dependent formate dehydrogenases

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The prokaryotic formate metabolism is considerably diversified. Prokaryotes use formate in the C1 metabolism, but also evolved to exploit the low reduction potential of formate to derive energy, by coupling its oxidation to the reduction of numerous electron acceptors. To fulfil these varied physiological roles, different types of formate dehydrogenase (FDH) enzymes have evolved to catalyse the reversible 2-electron oxidation of formate to carbon dioxide. This review will highlight our present knowledge about the diverse physiological roles of FDH in prokaryotes, their modular structural organisation and active site structures and the mechanistic strategies followed to accomplish the formate oxidation. In addition, the ability of FDH to catalyse the reverse reaction of carbon dioxide reduction, a potentially relevant reaction for carbon dioxide sequestration, will also be addressed. © 2014 SBIC.
Original languageEnglish
Pages (from-to)287-309
Number of pages23
JournalJBIC Journal of Biological Inorganic Chemistry
Issue number2
Publication statusPublished - Mar 2015
Event2013 Molybdenum and Tungsten Enzymes Conference - Sintra, Portugal
Duration: 16 Jul 201319 Jul 2013


  • Carbon dioxide reduction
  • Formate oxidation
  • Formate-dependent energy metabolism
  • Molybdenum
  • Sulfur-shift
  • Tungsten


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