[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 journalArticle

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Abstract

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.

LanguageEnglish (US)
Pages181-196
Number of pages16
JournalJournal of Molecular Microbiology and Biotechnology
Volume10
Issue number2-4
DOIs
StatePublished - Apr 2006
Externally publishedYes

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Cupriavidus necator
Hydrogenase
Hydrogen
Enzymes
Oxygen
Oxidation
Signal transduction
Biosynthesis
Transcription
Genes
Spectroscopy
Membranes
Catalysts
Electron Transport
NAD
asoxime chloride
nickel-iron hydrogenase
Signal Transduction
Spectrum Analysis
Research

Keywords

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

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Microbiology
  • Bioengineering

Cite this

[NiFe]-hydrogenases of Ralstonia eutropha H16 : Modular enzymes for oxygen-tolerant biological hydrogen oxidation. / Burgdorf, Tanja; Lenz, Oliver; Buhrke, Thorsten; Van Der Linden, Eddy; Jones, Anne K.; Albracht, Simon P J; Friedrich, Bärbel.

In: Journal of Molecular Microbiology and Biotechnology, Vol. 10, No. 2-4, 04.2006, p. 181-196.

Research output: Contribution to journalArticle

Burgdorf, Tanja ; Lenz, Oliver ; Buhrke, Thorsten ; Van Der Linden, Eddy ; Jones, Anne K. ; Albracht, Simon P J ; Friedrich, Bärbel. / [NiFe]-hydrogenases of Ralstonia eutropha H16 : Modular enzymes for oxygen-tolerant biological hydrogen oxidation. In: Journal of Molecular Microbiology and Biotechnology. 2006 ; Vol. 10, No. 2-4. pp. 181-196
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