Abstract
The effect of various nucleotides on the Fe-containing component of nitrogenase of Klebsiella pneumoniae was investigated by ultracentrifugation and thiol-group reactivity towards 5,5′-dithiobis-(2-nitrobenzoate). In the absence of Na2S2O4, ATP and ADP produced changes in sedimentation behaviour and thiol-group reactivity consistent with association of the protein.
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