EPR experiments to elucidate the structure of the ready and unready states of the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F. (1st February 2005)

• Record Type: Journal Article
• Authors: van Gastel, M.; Fichtner, C.; Neese, F.; Lubitz, W.
• Is Part Of: Biochemical Society transactions. Volume 33:Number 1(2005)
• Page Start: 7
• Page End: 11
• Publication Date: 2005-02-01
• Subjects: Desulfovibrio vulgaris Miyazaki F -- density functional theory (DFT) -- electron nuclear double resonance (ENDOR) -- EPR -- hydrogenase -- hyperfine sublevel correlation (HYSCORE); Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0330007
• Languages: English
• ISSNs: 0300-5127

Abstract

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 1 H 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.