Volume 52, Issue 38 pp. 10116-10119
Communication

Analysis of the Magnetic Properties of Nitrogenase FeMo Cofactor by Single-Crystal EPR Spectroscopy

Dr. Thomas Spatzal

Dr. Thomas Spatzal

Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg (Germany) http://portal.uni-freiburg.de/biochemie

BIOSS Centre for Biological Signalling Studies, Hebelstrasse 25, 79104 Freiburg (Germany)

Present address: Howard Hughes Medical Institute (HHMI) and Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, Pasadena CA 91125 (USA)

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Prof. Oliver Einsle

Corresponding Author

Prof. Oliver Einsle

Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg (Germany) http://portal.uni-freiburg.de/biochemie

BIOSS Centre for Biological Signalling Studies, Hebelstrasse 25, 79104 Freiburg (Germany)

Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg (Germany) http://portal.uni-freiburg.de/biochemie===Search for more papers by this author
Prof. Susana L. A. Andrade

Corresponding Author

Prof. Susana L. A. Andrade

Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg (Germany) http://portal.uni-freiburg.de/biochemie

BIOSS Centre for Biological Signalling Studies, Hebelstrasse 25, 79104 Freiburg (Germany)

Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg (Germany) http://portal.uni-freiburg.de/biochemie===Search for more papers by this author
First published: 08 August 2013
Citations: 24

This work was supported by Deutsche Forschungsgemeinschaft (grant AN 676/3 to S.L.A.A., grant EI 520/7 to O.E.) and the European Research Council.

Graphical Abstract

The catalytic center of nitrogenase, the [Mo:7Fe:9S:C]:homocitrate FeMo cofactor, is a S=3/2 system with a rhombic magnetic g tensor. Single-crystal EPR spectroscopy in combination with X-ray diffraction were used to determine the relative orientation of the g 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.

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