Premium
EPR of a novel high‐spin component in activated hydrogenase from Desulfovibrio vulgaris (Hildenborough)
Author(s) -
Hagen W.R.,
van Berkel-Arts A.,
Krüse-Wolters K.M.,
Dunham W.R.,
Veeger C.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80590-7
Subject(s) - desulfovibrio vulgaris , hydrogenase , electron paramagnetic resonance , chemistry , desulfovibrio , spin (aerodynamics) , iron–sulfur cluster , crystallography , nuclear magnetic resonance , physics , enzyme , biochemistry , bacteria , biology , organic chemistry , genetics , sulfate , thermodynamics
The EPR of reoxidized hydrogenase from Desulfovibrio vulgaris (H.) has been reinvestigated. In contrast to other workers [(1984) Proc. Natl. Acad. Sci. USA 81, 3728‐3732] we find the axial signal with g = 2.06; 2.01 to be only a minor component of concentration 0.03 . In the spectrum of fully active reoxidized enzyme this signal is overshadowed by a rhombic signal (0.1 ) with g = 2.11; 2.05; 2.00 reminiscent of the only signal found for other oxidized bidirectional hydrogenases. In addition, a novel signal has been detected with g eff = 5.0 which, under the assumptions that S = 2 and ¦Δ m s ¦= 2, quantitates to roughly one . Ethylene glycol affects the relative intensity of the different signals. It is suggested that O 2 sensitization parallels a spin‐state transition of an iron‐sulfur cluster.