The molybdenum and iron-sulphur centres of Escherichia coli nitrate reductase are non-randomly oriented in the membrane
Blum, H.; Poole, R.K.
Biochemical and Biophysical Research Communications 107(3): 903-909
1982
ISSN/ISBN: 0006-291X PMID: 6291520 Document Number: 196342
Oriented membrane multilayers, prepared from E. coli grown anaerobically with nitrate, allowed the spatial organization of EPR detectable signals from the respiratory nitrate reductase (EC 1.7.99.4) to be examined. At low temperatures (7.degree. K), 2 signals (g = 2.02, g = 1.98) have been assigned to an Fe-S cluster and their magnitudes were dependent on the angle that the multilayer makes with the magnetic field of the EPR spectrometer. Signals seen at 45.degree. K (g = 1.985, g = 1.96) were attributed to an anisotropic Mo center. These redox components of the nitrate reductase are thus non-randomly oriented in the cytoplasmic membrane.