Studies on Chemical Composition of Iron-molybdenum Cofactor from Nitrogenase by Fluorescence Analysis

The iron molybdenum cofactor (FeMoco) of nitrogenase MoFe-protein from Azotobacter vinelandii OP was extracted by N-methylformamide(NMF). The effects of FeMoco(in NMF) on electronic spectrum and fluorescence intensity of fluorescein dimercury acetate(FDMA)(in 1 mol/L NaOH) were investigated by fluorophotometric titrations and compared with those of (NH4)2MoS4 and complexes of (NH4)2MoS4 with Na2S or Na2S2 or (NH4)2Sx on the relative properties of FDMA. It was found that the electronic spectrum of FDMA displayed hypsochromic shift(17 nm) in the presence of FeMoco just like that in the presence of other inorganic sulfides and that the titration curve for the quench of FDMA with FeMoco is very similar to that for the quench of FDMA with complex of (NH4)2MoS4 with Na2S2(mole ratio is 1∶3).

The results showed that FeMoco(N) probably contained S—S bonds and its structure was found to be changed compared with Kim-Rees structural model. This change should profit the formation of the polymer.

 

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