Imperial J, Shah V K, Ugalde R A, Ludden P W, Brill W J
J Bacteriol. 1987 Apr;169(4):1784-6. doi: 10.1128/jb.169.4.1784-1786.1987.
Nif- mutants of Azotobacter vinelandii defective in dinitrogenase activity synthesized iron-molybdenum cofactor (FeMo-co) and accumulated it in two protein-bound forms: inactive dinitrogenase and a possible intermediate involved in the FeMo-co biosynthetic pathway. FeMo-co from both these proteins could activate apo-dinitrogenase from FeMo-co-deficient mutants.
维涅兰德固氮菌中缺乏固氮酶活性的Nif-突变体合成了铁钼辅因子(FeMo-co),并以两种蛋白质结合形式积累:无活性的固氮酶和FeMo-co生物合成途径中可能的中间体。来自这两种蛋白质的FeMo-co都可以激活FeMo-co缺陷型突变体中的脱辅基固氮酶。