Further characterization of the spin coupling observed in oxidized hydrogenase from Chromatium vinosum. A mossabauer and multifrequency EPR study

Authors :: Surerus, Kristene K.
Chen, Min
Zwaan, J. Wim van der
Rusnak, Frank M.
Kolk, Michael
Duin, Evert C.
Albracht, Simon P.J.
Munck, Eckard
Source :: Biochemistry. April 26, 1994, Vol. 33 Issue 16, p4980, 14 p.
Publication Year :: 1994
Abstract: Hydrogenase enzymes from Chromatium vinosum have one Fe3S4 and two Fe4S4 clusters. This is revealed during Mossbauer and EPR studies of the enzyme. The hydrogenase enzyme is synthesized in four different states of oxidation. The two Fe4S4 clusters have the same Mossbauer parameters in their oxidized states.

Subjects :: Enzymes -- Research
Spectrum analysis -- Observations
Biological sciences
Chemistry

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