Biosynthesis of the Iron-Molybdenum Cofactor of Nitrogenase

· 102 Rubio Ludden reactions was required to achieve homocitrate incorporation in vitro, and we propose that the actual incorporation of homocitrate into the FeMo-co precursor would take place in the scaffold protein NifEN while associated with NifH

Luis M. Rubio; Paul W. Ludden

2008

Scholarcy highlights

  • NifDK NifH ilar subunit and cofactor composition
  • · 102 Rubio Ludden reactions was required to achieve homocitrate incorporation in vitro, and we propose that the actual incorporation of homocitrate into the FeMo-co precursor would take place in the scaffold protein NifEN while associated with NifH
  • Given that NifX binds a variety of structurally related cofactors, and exchanges some of them with NifEN, it would not be surprising that NifX accumulated an excess of molybdenum-containing FeMo-co precursor in reactions lacking homocitrate
  • NifX and NafY addition stimulated the efficiency of FeMo-co biosynthesis, and the addition of the appropriate chemical forms of homocitrate, iron, sulfur, and molybdenum could substitute for the roles played in vivo by NifV, NifS, NifU, and NifQ
  • The availability of all proteins involved in FeMo-co biosynthesis and insertion, in purified form, is providing the first insights into the structures of the FeMo-co biosynthetic intermediates
  • The central six-iron-atom cage of FeMo-co already exists at the stage of NifB-co, which exhibits the spectroscopic signature that has been attributed to a central atom X in FeMo-co

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