Abstract
The activation of inactive Fe-protein from Rhodospirillum rubrum is dependent on the presence of ATP and a divalent cation. By preactivation of inactive Fe-protein in the presence of activating enzyme, ATP and different divalent cations, the efficiency of the metal ions used was studied. Mn 2+, as the only divalent cation present, will support maximal rate of activation in vitro. Mn 2+ is reqired both as free ion and as MnATP. MgATP will function as the meta(II)-nucleotide needed, but Mg 2+ is a poor activator as free ion. Fe + alone can support activation to the same extent as Mn 2+. It was also found that Ba 2+ is a competitive inhibitor versus Mn 2+ in the activation but has little effect on acetylene reduction by nitrogenase when active Fe-protein is used.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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