Abstract
Nitrogenase MoFe protein is routinely isolated from the cytoplasmic fraction of disrupted cells and, clearly, is not an intrinsic membrane protein. However, evidence does exist for extrinsic structural and functional interactions between MoFe protein and membrane in several organisms. Nitrogenase activity and, specifically, MoFe protein can be found in the pellets of osmotically lysed A. vinelandii and chromatophore preparations of osmotically lysed R. rubrum, respectively; MoFe protein has been localized in the vicinity of the cell membrane in A. vinelandii by immuno- ferritin labeling; and in situ nitrogenase activity has been shown to be enhanced by the presence of an intact energized membrane. We have used electron spin resonance (esr) spectroscopy and spatially oriented whole bacterial systems to obtain evidence for a structural association between MoFe protein and membrane in A. vinelandii, R. rubrum, and to a lesser extent, in Rhodopseudomonas palustris.
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