Abstract
X-ray magnetic circular dichroism (XMCD) is the asymmetric absorption of left- and right-handed circularly polarized x rays and can be used to measure element-specific spin and oxidation states and magnetic moments. We have built an end station for XMCD spectroscopy to study transition metals located in the active sites of proteins and inorganic model compounds. The instrument is equipped with a 6 T superconducting magnet and a liquid helium cooled sample stage designed for experiments at temperatures as low as 2.2 K and beyond 160 K. Sample heating by infrared radiation is minimized using a liquid helium cooled heat shield with 100-nm-thick Al windows. We demonstrate the capabilities of the apparatus in a total electron yield study on the model compound [(F8–TPP)Fe–O–Cu(TMPA)]+. We show that Fe and Cu are antiferromagnetically coupled by comparing the polarity of the XMCD signal at the respective L-edges. We discuss the capability of the instrument to study dilute (<1000 ppm) transition metals in proteins using partial fluorescence yield.
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