Analysis of the Magnetic Properties of Nitrogenase FeMo Cofactor by Single‐Crystal EPR Spectroscopy1. Issue 38 (8th August 2013)

• Record Type: Journal Article
• Authors: Spatzal, Thomas; Einsle, Oliver; Andrade, Susana L. A.
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 38(2013)
• Page Start: 10116
• Page End: 10119
• Publication Date: 2013-08-08
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201303000
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The catalytic center</bold> of nitrogenase, the [Mo:7Fe:9S:C]:homocitrate FeMo cofactor, is a <italic>S</italic>=3/2 system with a rhombic magnetic <bold>g</bold> tensor. Single‐crystal EPR spectroscopy in combination with X‐ray diffraction were used to determine the relative orientation of the <bold>g</bold> tensor with respect to the cluster structure. The protein environment influences the electronic structure of the FeMo cofactor, dictating preferred orientations of possible functional relevance.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg37r9mj2w" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>