Abstract
Soluble nitrogenase from Rhodospirillum rubrum has been isolated and separated into its two components, the MoFe protein and the Fe protein. The MoFe protein has been purified to near homogeneity and has a molecular weight of 215 000. It contains two Mo, 25–30 Fe and 19–22 acid-labile sulphide and consists of four subunits, M w 56 000. The Fe protein has a molecular weight of 65 000. It contains approximately four Fe and four acidlabile sulphide and consists of two subunits, M w 31 500. The highest specific activities for the purified components are 920 and 1260 nmol ethylene produced per min per mg protein, respectively. The purified components require the membrane component for activity (Nordlund, S., Eriksson, U. and Baltscheffsky, H. (1977) Biochim. Biophys. Acta 462, 187–195). Titration of the MoFe protein with the Fe protein shows saturation and excess MoFe protein over Fe protein is inhibitory. Addition of Fe 2+ or Mn 2+ to the reaction mixture increases the activity apparently through interaction with the membrane component.
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