EPR Investigation of [NiFe] Hydrogenases

  • Maurice van Gastel
  • Wolfgang Lubitz
Part of the Biological Magnetic Resonance book series (BIMR, volume 28)

EPR studies of the [NiFe] hydrogenases are reviewed. These enzymes contain a heterobimetallic [NiFe] center as the active site. The nickel is ligated to four cysteine residues, two of which form a bridge to the iron. The iron carries additionally 3 small inorganic diatomic ligands (2CN, CO). A third small ligand X is situated in the bridge between Ni and Fe. In the catalytic cycle the enzyme passes through a number of redox states, several of which are paramagnetic. The iron remains in the divalent low-spin (FeII, S = 0) state, whereas the nickel changes its valence and spin state during this cycle. Nickel is believed to bind the hydrogen and to be directly involved in the catalytic process.


Spin Density Midpoint Potential Spin Density Distribution HYSCORE Spectrum Biol Inorg 
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© Springer-Verlag New York 2009

Authors and Affiliations

  1. 1.Max-Planck-Institut für Bioanorganische Chemie, Mülheim an der RuhrMülheim an der RuhrGermany

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