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High Resolution EPR pp 441–470Cite as

EPR Investigation of [NiFe] Hydrogenases

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Part of the book series: Biological Magnetic Resonance ((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.

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  1. Max-Planck-Institut für Bioanorganische Chemie, Mülheim an der Ruhr, Mülheim an der Ruhr, Germany

    Maurice van Gastel & Wolfgang Lubitz

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  1. Maurice van Gastel
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  2. Wolfgang Lubitz
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Correspondence to Maurice van Gastel .

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    van Gastel, M., Lubitz, W. (2009). EPR Investigation of [NiFe] Hydrogenases. In: Berliner, L., Hanson, G. (eds) High Resolution EPR. Biological Magnetic Resonance, vol 28. Springer, New York, NY. https://doi.org/10.1007/978-0-387-84856-3_10

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