Low temperature magnetic circular dichroism spectroscopy as a probe for the optical transitions of paramagnetic nickel in hydrogenase

A partially-purified sample of hydrogenase from Methanobacterium thermoautotrophicum (ΔH strain) has been investigated by optical absorption, magnetic circular dichroism and electron paramagnetic resonance spectroscopy. Variable temperature magnetic circular dichroism studies reveal, for the first t...

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Veröffentlicht in:Biochemical and biophysical research communications 1985-04, Vol.128 (1), p.220-225
Hauptverfasser: Johnson, Michael K., Zambrano, Isabel C., Czechowski, Melvin H., Peck, Harry D., DerVartanian, Daniel V., LeGall, Jean
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Sprache:eng
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Zusammenfassung:A partially-purified sample of hydrogenase from Methanobacterium thermoautotrophicum (ΔH strain) has been investigated by optical absorption, magnetic circular dichroism and electron paramagnetic resonance spectroscopy. Variable temperature magnetic circular dichroism studies reveal, for the first time, the optical transitions associated with the Ni(III) center in the oxidized enzyme. Low temperature magnetic circular dichroism spectroscopy provides a new method of assessing both the coordination environment of Ni in hydrogenase and the appropriateness of inorganic model complexes.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(85)91667-5