Activation of a [NiFe]-hydrogenase-4 isoenzyme by maturation proteases

Alexander J. Finney, Grant Buchanan, Tracy Palmer, Sarah J. Coulthurst, Frank Sargent (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)
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Maturation of [NiFe]-hydrogenases often involves specific proteases responsible for cleavage of the catalytic subunits. Escherichia coli HycI is the protease dedicated to maturation of the Hydrogenase-3 isoenzyme, a component of formate hydrogenlyase-1. In this work, it is demonstrated that a Pectobacterium atrosepticum HycI homologue, HyfK, is required for hydrogenase-4 activity, a component of formate hydrogenlyase-2, in that bacterium. The P. atrosepticum ΔhyfK mutant phenotype could be rescued by either P. atrosepticum hyfK or E. coli hycI on a plasmid. Conversely, an E. coli ΔhycI mutant was complemented by either E. coli hycI or P. atrosepticum hyfK in trans. E. coli is a rare example of a bacterium containing both hydrogenase-3 and hydrogenase-4, however the operon encoding hydrogenase-4 has no maturation protease gene. This work suggests HycI should be sufficient for maturation of both E. coli formate hydrogenlyases, however no formate hydrogenlyase-2 activity was detected in any E. coli strains tested here.

Original languageEnglish
Pages (from-to)854-860
Number of pages7
Issue number9
Early online date30 Jul 2020
Publication statusPublished - 2020


  • Escherichia coli
  • Pectobacterium atrosepticum
  • formate hydrogenlyase
  • hydrogenase
  • maturase
  • protease
  • Hydrogenase
  • Formate hydrogenlyase
  • Protease
  • Maturase

ASJC Scopus subject areas

  • Microbiology


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