Specificity and selectivity of HypC chaperonins and endopeptidases in the molecular assembly machinery of [NiFe] hydrogenases of Thiocapsa roseopersicina

Gergely Maróti, Gábor Rákhely, Judit Maróti, Emma Dorogházi, Eva Klement, Katalin F. Medzihradszky, Kornél L. Kovács

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The purple photosynthetic bacterium, Thiocapsa roseopersicina harbours at least three functional [NiFe] hydrogenases. Two of them are attached to the periplasmic membrane (HynSL, HupSL), while the third one is apparently localized in the cytoplasm (HoxEFUYH). Two hypC-type genes, coding for putative small maturation proteins, were found and their roles were studied by activity measurements performed with hypC mutants. Protein-protein interaction experiments confirmed that each HypC-type protein participates in the maturation of at least two [NiFe] hydrogenase large subunits via direct interaction. Endopeptidases perform the last step of the complex [NiFe] hydrogenase maturation process. A separate endopeptidase (HynD, HupD, HoxW) cleaves off the C-terminus of each large subunit and they are strictly specific for their corresponding hydrogenases. The results demonstrate a sophisticated assembly of these functionally active redox metalloenzymes through specific and selective protein-protein interactions and imply some diversity in the hydrogenase assembly machinery among the various microbes.

Original languageEnglish
Pages (from-to)3358-3370
Number of pages13
JournalInternational Journal of Hydrogen Energy
Issue number8
Publication statusPublished - Apr 1 2010



  • Auxiliary proteins
  • Biohydrogen
  • Protein-protein interaction
  • [NiFe] hydrogenase

ASJC Scopus subject areas

  • Renewable Energy, Sustainability and the Environment
  • Fuel Technology
  • Condensed Matter Physics
  • Energy Engineering and Power Technology

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