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Structural Features of the Unready Ni-A State of [NiFe] Hydrogenase Revealed by X-Ray Crystallography and EPR Spectroscopy

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Abstract

The oxidized “unready” Ni-A state [NiFe] hydrogenases has been the subject of recent investigations by spectroscopic and crystallographic techniques. In the Ni-A state, the enzyme is inhibited and cannot turn over molecular hydrogen. Ideally, if the Ni-A state can be avoided, and if the oxidized enzyme exclusively resides in the “ready” Ni-B state, it can be quickly activated, thus increasing its activity of hydrogen production. In this study, recent observations by electron paramagnetic resonance spectroscopy as well as X-ray crystallography are combined and interpreted. Though it remains a mystery as to which differences exist on the geometric and electronic level between the Ni-A and Ni-B states, and in particular about the exact structure of the active site in the Ni-A state, the recent studies when combined do provide important hints.

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Acknowledgments

The author thanks Prof. Dr. Wolfgang Lubitz for a fruitful and enjoyable six-year collaboration in his laboratories, for his help and kind advice both inside and outside the laboratories and for his hospitality.

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Correspondence to Maurice van Gastel.

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van Gastel, M. Structural Features of the Unready Ni-A State of [NiFe] Hydrogenase Revealed by X-Ray Crystallography and EPR Spectroscopy. Appl Magn Reson 37, 207–218 (2010). https://doi.org/10.1007/s00723-009-0044-0

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  • DOI: https://doi.org/10.1007/s00723-009-0044-0

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