Published September 16, 2013
| Supplemental Material
Journal Article
Open
Analysis of the Magnetic Properties of Nitrogenase FeMo Cofactor by Single-Crystal EPR Spectroscopy
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.
Additional Information
© 2013 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. Issue online: 12 September 2013; Version of record online: 8 August 2013; Manuscript Revised: 11 June 2013; Manuscript Received: 10 April 2013. 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.Attached Files
Supplemental Material - anie_201303000_sm_miscellaneous_information.pdf
Files
anie_201303000_sm_miscellaneous_information.pdf
Files
(2.6 MB)
| Name | Size | Download all |
|---|---|---|
|
md5:6dd9aec9cc73efc8f91bfe55501ffe63
|
2.6 MB | Preview Download |
Additional details
- Eprint ID
- 75538
- DOI
- 10.1002/anie.201303000
- Resolver ID
- CaltechAUTHORS:20170330-082549882
- AN 676/3
- Deutsche Forschungsgemeinschaft (DFG)
- EI 520/7
- Deutsche Forschungsgemeinschaft (DFG)
- European Research Council (ERC)
- Created
-
2017-03-30Created from EPrint's datestamp field
- Updated
-
2021-11-15Created from EPrint's last_modified field