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

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 Trans

authors

van Gastel M,Fichtner C,Neese F,Lubitz W

doi

10.1042/BST0330007

keywords:

subject

Has Abstract

pub_date

2005-02-01 00:00:00

pages

7-11

issue

Pt 1

eissn

0300-5127

issn

1470-8752

pii

BST0330007

journal_volume

33

pub_type

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