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Low temperature magnetic circular dichroism spectroscopy as a probe for the optical transitions of paramagnetic nickel in hydrogenase |
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| Authors: | M K Johnson I C Zambrano M H Czechowski H D Peck D V DerVartanian J LeGall |
| Affiliation: | Department of Physics and Astronomy State University of New York at Buffalo Buffalo, New York 14260, USA |
| Abstract: | A partially-purified sample of hydrogenase from Methanobacterium thermoautotrophicum (delta H 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. |
| Keywords: | POPS 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine OSPC 1-oleoyl-2-stearoyl-sn-glycero-3-phosphocholine PSPC 1-palmitoyl-2-stearoyl-sn-glycero-3-phosphocholine SPPC 1-stearoyl-2-palmitoyl-sn-glycero-3-phosphocholine DNPC L-α-dinervonoyl-phosphatidylcholine |
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