Nitrogenase X: Mössbauer and EPR studies on reversibly oxidized MoFe protein from Azotobacter vinelandii OP. Nature of the iron centers.
Zimmermann, R
Nitrogenase X: Mössbauer and EPR studies on reversibly oxidized MoFe protein from Azotobacter vinelandii OP. Nature of the iron centers. [electronic resource] - Biochimica et biophysica acta Dec 1978 - 185-207 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
0006-3002
10.1016/0005-2795(78)90504-4 doi
Azotobacter--enzymology
Clostridium--enzymology
Electron Spin Resonance Spectroscopy
Iron
Klebsiella pneumoniae--enzymology
Metalloproteins
Molybdenum
Nitrogenase
Oxidation-Reduction
Protein Binding
Protein Conformation
Species Specificity
Spectrum Analysis
Nitrogenase X: Mössbauer and EPR studies on reversibly oxidized MoFe protein from Azotobacter vinelandii OP. Nature of the iron centers. [electronic resource] - Biochimica et biophysica acta Dec 1978 - 185-207 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
0006-3002
10.1016/0005-2795(78)90504-4 doi
Azotobacter--enzymology
Clostridium--enzymology
Electron Spin Resonance Spectroscopy
Iron
Klebsiella pneumoniae--enzymology
Metalloproteins
Molybdenum
Nitrogenase
Oxidation-Reduction
Protein Binding
Protein Conformation
Species Specificity
Spectrum Analysis