[NiFe]-hydrogenases of Ralstonia eutropha H16: Modular enzymes for oxygen-tolerant biological hydrogen oxidation

Tanja Burgdorf, Oliver Lenz, Thorsten Buhrke, Eddy Van Der Linden, Anne K. Jones, Simon P.J. Albracht, Bärbel Friedrich

Research output: Contribution to journalShort surveypeer-review

185 Scopus citations


Recent research on hydrogenases has been notably motivated by a desire to utilize these remarkable hydrogen oxidation catalysts in biotechnological applications. Progress in the development of such applications is substantially hindered by the oxygen sensitivity of the ma-jority of hydrogenases. This problem tends to inspire the study of organisms such as Ralstonia eutropha H16 that produce oxygen-tolerant [NiFe]-hydrogenases. R. eutropha H16 serves as an excellent model system in that it produces three distinct [NiFe]-hydrogenases that each serve unique physiological roles: a membrane-bound hydrogenase (MBH) coupled to the respiratory chain, a cytoplasmic, soluble hydrogenase (SH) able to generate reducing equivalents by reducing NAD+ at the expense of hydrogen, and a regulatory hydrogenase (RH) which acts in a signal transduction cascade to control hydrogenase gene transcription. This review will present recent results regarding the biosynthesis, regulation, structure, activity, and spectroscopy of these enzymes. This information will be discussed in light of the question how do organisms adapt the prototypical [NiFe]-hydrogenase system to function in the presence of oxygen.

Original languageEnglish (US)
Pages (from-to)181-196
Number of pages16
JournalJournal of Molecular Microbiology and Biotechnology
Issue number2-4
StatePublished - Apr 1 2006
Externally publishedYes


  • H sensing
  • Hydrogenase maturation
  • Metal center assembly
  • NADH dehydrogenase
  • Ni-Fe-active site
  • Protein complexes
  • Two-component system
  • [NiFe]-hydrogenases

ASJC Scopus subject areas

  • Biotechnology
  • Microbiology
  • Applied Microbiology and Biotechnology
  • Molecular Biology


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