A second soluble hox-type NiFe enzyme completes the hydrosenase set in thiocapsa roseopersicina BBS

Judit Maróti, Attila Farkas, Ildikó K. Nagy, Gergely Maróti, Éva Kondorosi, Gábor Rákhely, Kornél L. Kovács

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Three functional NiFe hydrogenases were previously characterized in Thiocapsa roseopersicina BBS: two of them are attached to the periplasmic membrane (HynSL and HupSL), and one is localized in the cytoplasm (HoxEFUYH). The ongoing genome sequencing project revealed the presence of genes coding for another soluble Hox-type hydrogenase enzyme (hox2FUYH). Hox2 is a heterotetrameric enzyme; no Indication for an additional subunit was found. Detailed comparative in vivo and in vitro activity and expression analyses of HoxEFUYH (Hox1) and the newly discovered Hox2 enzyme were performed. Functional differences between the two soluble NiFe hydrogenases were disclosed. Hoxl seems to be connected to both sulfur metabolism and dark/photofermentative processes. The bidirectional Hox2 hydrogenase was shown to be metabolically active under specific conditions: it can evolve hydrogen in the presence of glucose at low sodium thiosulfate concentration. However, under nitrogen-fixing conditions, it can oxidize H2 but less than the other hydrogenases in the cell.

Original languageEnglish
Pages (from-to)5113-5123
Number of pages11
JournalApplied and environmental microbiology
Volume76
Issue number15
DOIs
Publication statusPublished - Aug 1 2010

ASJC Scopus subject areas

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

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