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- W2079776554 abstract "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. Mn2+, as the only divalent cation present, will support maximal rate of activation in vitro. Mn2+ is reqired both as free ion and as MnATP. MgATP will function as the meta(II)-nucleotide needed, but Mg2+ is a poor activator as free ion. Fe+ alone can support activation to the same extent as Mn2+. It was also found that Ba2+ is a competitive inhibitor versus Mn2+ in the activation but has little effect on acetylene reduction by nitrogenase when active Fe-protein is used." @default.
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- W2079776554 date "1984-11-01" @default.
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- W2079776554 title "Dependence on divalent cations of the activation of inactive Fe-protein of nitrogenase from rhodospirillum rubrum" @default.
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- W2079776554 doi "https://doi.org/10.1016/0167-4838(84)90276-0" @default.
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