The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre

@article{Fritsch2011TheCS,
  title={The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre},
  author={Johannes Fritsch and Patrick Scheerer and Stefan Frielingsdorf and Sebastian Kroschinsky and B. Cornelia Friedrich and Oliver Lenz and Christian Spahn},
  journal={Nature},
  year={2011},
  volume={479},
  pages={249-252}
}
Hydrogenases are abundant enzymes that catalyse the reversible interconversion of H2 into protons and electrons at high rates. Those hydrogenases maintaining their activity in the presence of O2 are considered to be central to H2-based technologies, such as enzymatic fuel cells and for light-driven H2 production. Despite comprehensive genetic, biochemical, electrochemical and spectroscopic investigations, the molecular background allowing a structural interpretation of how the catalytic centre… CONTINUE READING
Related Discussions
This paper has been referenced on Twitter 9 times. VIEW TWEETS

From This Paper

Figures, tables, and topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 36 extracted citations

Design of artificial functional and regulatory systems in bacteria

Vorgelegt von Johannes Andreas Heinrich Maier aus Villingen Schwenningen, Deutschland Hauptberichter
2017
View 3 Excerpts
Highly Influenced

The hows and whys of aerobic H2 metabolism.

Current opinion in chemical biology • 2012
View 16 Excerpts
Highly Influenced

References

Publications referenced by this paper.
Showing 1-10 of 59 references

Aunique iron - sulfur cluster is crucial for oxygen toleranceof a [ NiFe ] - hydrogenase

T. Goris
Nature Chem . Biol . • 2011

Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus

Pandelia, E M.
Proc. Natl Acad. Sci. USA 108, • 2011

al.A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]hydrogenase

Goris, T.et
Nature Chem. Biol • 2011

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Acta crystallographica. Section D, Biological crystallography • 2010

Xds

Acta crystallographica. Section D, Biological crystallography • 2010

H 2 conversion in thepresence ofO 2 as performedby themembrane - bound [ NiFe ] - hydrogenaseof Ralstonia eutropha

O. Lenz
ChemPhysChem • 2010

Similar Papers

Loading similar papers…