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Analysis of the Magnetic Properties of Nitrogenase FeMo Cofactor by Single‐Crystal EPR Spectroscopy
Author(s) -
Spatzal Thomas,
Einsle Oliver,
Andrade Susana L. A.
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201303000
Subject(s) - nitrogenase , electron paramagnetic resonance , crystallography , single crystal , chemistry , cofactor , spectroscopy , nuclear magnetic resonance spectroscopy , computer science , nuclear magnetic resonance , materials science , physics , stereochemistry , quantum mechanics , enzyme , organic chemistry , nitrogen fixation , nitrogen
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.