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EPR experiments to elucidate the structure of the ready and unready states of the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F

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van Gastel,  M.
Research Department Lubitz, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society;

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Fichtner,  C.
Research Department Lubitz, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society;

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Neese,  F.
Research Department Wieghardt, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society;

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Lubitz,  W.
Research Department Lubitz, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society;

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Citation

van Gastel, M., Fichtner, C., Neese, F., & Lubitz, W. (2005). EPR experiments to elucidate the structure of the ready and unready states of the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F. Biochemical Society Transactions, 33(1), 7-11. doi:10.1042/BST0330007.


Cite as: https://hdl.handle.net/21.11116/0000-0008-38A1-3
Abstract
Isolation and purification of the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F under aerobic conditions leads to a mixture of two states, Ni-A (unready) and Ni-B (ready). The two states are distinguished by different activation times and different EPR spectra. HYSCORE and ENDOR data and DFT calculations show that both states have an exchangeable proton, albeit with a different 1H hyperfine coupling. This proton is assigned to the bridging ligand between Ni and Fe. For Ni-B, a hydroxo ligand is found. For Ni-A, either a hydroxo in a different orientation or a hydroperoxo-bridging ligand is present.