Quantitative EPR of an S = 7/2 system in thionine-oxidized MoFe proteins of nitrogenase. A redefinition of the P-cluster concept
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1987.tb13633.x/fullpdf
Reference36 articles.
1. Nitrogenase X: Mössbauer and EPR studies on reversibly oxidized MoFe protein from Azotobacter vinelandii OP Nature of the iron centers
2. The importance of quantitative Mossbauer spectroscopy of MoFe-protein from Azotobacter vinelandii
3. Nitrogenase. VIII. Mössbauer and EPR spectroscopy. The MoFe protein component from Azotobacter vinelandii OP
4. Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase.
5. Characterization of the paramagnetic centres of the molybdenum-iron protein of nitrogenase from Klebsiella pneumoniae using low temperature magnetic circular dichroism spectroscopy
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