Ligand discrimination of myoglobin in solution: an iron L-edge X-ray absorption study of the active centre

Kathrin M. Lange; Ronny Golnak; Sébastien Bonhommeau; Emad F. Aziz

doi:10.1039/C3CC37973F

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Chemical Communications

Issue 39, 2013

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Communication

Ligand discrimination of myoglobin in solution: an iron L-edge X-ray absorption study of the active centre

Kathrin M. Lange,^a Ronny Golnak,^b Sébastien Bonhommeau^d and Emad F. Aziz*^b^c

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Corresponding authors

Max-Born-Institut, Max Born Straße 2A, 12489 Berlin, Germany
E-mail: kathrin.lange@mbi-berlin.de ;
Tel: +49 30 63921248

Joint Ultrafast Dynamics Lab in Solutions and at Interfaces (JULiq), Helmholtz-Zentrum Berlin für Materialien und Energie, Albert-Einstein-Str 15, 12489 Berlin, Germany

Freie Universität Berlin, FB Physik, Arnimallee 14, D-14195 Berlin, Germany
E-mail: emad.aziz@helmholtz-berlin.de ;
Tel: +49 30806215003

Université de Bordeaux, Institut des Sciences Moléculaires, CNRS UMR 5255, F-33400 Talence, France

Chem. Commun., 2013,49, 4163-4165

DOI: 10.1039/C3CC37973F
Received 03 Nov 2012, Accepted 04 Feb 2013
First published online 05 Feb 2013

This article is part of themed collection: Emerging Investigators 2013

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Abstract
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Iron L-edge X-ray absorption spectra of the active centre of myoglobin in the met-form, in the reduced form and upon ligation to O₂, CO, NO and CN are presented. The strength of ligation with the iron centre is finger-printed through the variation of the L₃:L₂ intensity ratio. Charge Transfer Multiplet calculations are performed and give qualitative information about oxidation states as well as charge transfer.