Growth- and substrate-dependent transcription of formate dehydrogenase and hydrogenase coding genes in Syntrophobacter fumaroxidans and Methanospirillum hungatei

P. Worm, A.J.M. Stams, X. Cheng, C.M. Plugge

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51 Citations (Scopus)

Abstract

Transcription of genes coding for formate dehydrogenases (fdh genes) and hydrogenases (hyd genes) in Syntrophobacter fumaroxidans and Methanospirillum hungatei was studied following growth under different conditions. Under all conditions tested, all fdh and hyd genes were transcribed. However, transcription levels of the individual genes varied depending on the substrate and growth conditions. Our results strongly suggest that in syntrophically grown S. fumaroxidans cells, the [FeFe]-hydrogenase (encoded by Sfum_844-46), FDH1 (Sfum_2703-06) and Hox (Sfum_2713-16) may confurcate electrons from NADH and ferredoxin to protons and carbon dioxide to produce hydrogen and formate, respectively. Based on bioinformatic analysis, a membrane-integrated energy-converting [NiFe]-hydrogenase (Mhun_1741-46) of M. hungatei might be involved in the energy-dependent reduction of CO2 to formylmethanofuran. The best candidates for F420-dependent N5,N10-methyl-H4 MPT and N5,N10,-methylene-H4MPT reduction are the cytoplasmic [NiFe]-hydrogenase and FDH1. 16S rRNA ratios indicate that in one of the triplicate co-cultures of S. fumaroxidans and M. hungatei, less energy was available for S. fumaroxidans. This led to enhanced transcription of genes coding for the Rnf-complex (Sfum_2694-99) and of several fdh and hyd genes. The Rnf-complex probably reoxidized NADH with ferredoxin reduction, followed by ferredoxin oxidation by the induced formate dehydrogenases and hydrogenases
Original languageEnglish
Pages (from-to)280-289
JournalMicrobiology
Volume157
Issue number1
DOIs
Publication statusPublished - 2011

Keywords

  • sulfate-reducing bacterium
  • heterodisulfide reductase
  • syntrophic metabolism
  • methanogenic bacteria
  • propionate oxidation
  • escherichia-coli
  • archaea
  • genome
  • ferredoxin
  • cocultures

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