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.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
van Gastel M,Fichtner C,Neese F,Lubitz Wdoi
10.1042/BST0330007keywords:
subject
Has Abstractpub_date
2005-02-01 00:00:00pages
7-11issue
Pt 1eissn
0300-5127issn
1470-8752pii
BST0330007journal_volume
33pub_type
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