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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container_end_page 225
container_issue 1
container_start_page 220
container_title Biochemical and biophysical research communications
container_volume 128
creator Johnson, Michael K.
Zambrano, Isabel C.
Czechowski, Melvin H.
Peck, Harry D.
DerVartanian, Daniel V.
LeGall, Jean
description 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.
doi_str_mv 10.1016/0006-291X(85)91667-5
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source MEDLINE; ScienceDirect Journals (5 years ago - present)
subjects Applied sciences
Circular Dichroism
E.S.R
Electron Spin Resonance Spectroscopy
Euryarchaeota - enzymology
Exact sciences and technology
Hydrogenase
magnetic C.D
Methanobacterium thermoautrophicum
Nickel
Other techniques and industries
title Low temperature magnetic circular dichroism spectroscopy as a probe for the optical transitions of paramagnetic nickel in hydrogenase
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