Taxonomic distribution, structure/function relationship and metabolic context of the two families of sulfide dehydrogenases: SQR and FCSD

Filipe M. Sousa, Juliana G. Pereira, Bruno C. Marreiros, Manuela M. Pereira

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

Hydrogen sulfide (H2S) is a versatile molecule with different functions in living organisms: it can work as a metabolite of sulfur and energetic metabolism or as a signaling molecule in higher Eukaryotes. H2S is also highly toxic since it is able to inhibit heme cooper oxygen reductases, preventing oxidative phosphorylation. Due to the fact that it can both inhibit and feed the respiratory chain, the immediate role of H2S on energy metabolism crucially relies on its bioavailability, meaning that studying the central players involved in the H2S homeostasis is key for understanding sulfide metabolism. Two different enzymes with sulfide oxidation activity (sulfide dehydrogenases) are known: flavocytochrome c sulfide dehydrogenase (FCSD), a sulfide:cytochrome c oxidoreductase; and sulfide:quinone oxidoreductase (SQR). In this work we performed a thorough bioinformatic study of SQRs and FCSDs and integrated all published data. We systematized several properties of these proteins: (i) nature of flavin binding, (ii) capping loops and (iii) presence of key amino acid residues. We also propose an update to the SQR classification system and discuss the role of these proteins in sulfur metabolism.

Original languageEnglish
Pages (from-to)742-753
Number of pages12
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1859
Issue number9
DOIs
Publication statusPublished - 1 Sep 2018

Keywords

  • Flavocytochrome c
  • Flavoprotein
  • HS
  • Redox protein
  • Respiratory chain
  • Taxonomic profile

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