Abstract
The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of nitrogenase was investigated using the purified in vitro FeMo-co synthesis system and 99Mo. The purified system involves the addition of all components that are known to be required for FeMo-co synthesis in their purified forms. Here, we report the accumulation of a 99Mo-containing FeMo-co precursor on NifNE. Apart from NifNE, NifH and NifX also accumulate 99Mo label. We present evidence that suggests NifH may serve as the entry point for molybdenum incorporation into the FeMo-co biosynthetic pathway. We also present evidence suggesting a role for NifX in specifying the organic acid moiety of FeMo-co.
Highlights
Dinitrogenase (NifKD, MoFe-protein) and dinitrogenase reductase (NifH, Fe-protein) comprise the two-component complex metalloenzyme nitrogenase [1]
Apart from the above-mentioned gene products, NifV and NifQ are required during FeMo-co biosynthesis in vivo for the production of homocitrate and for a proposed molybdenum processing step, respectively [11, 27, 28]
We have studied the accumulation of 99Mo into proteins involved in the biosynthesis of FeMo-co
Summary
Dinitrogenase (NifKD, MoFe-protein) and dinitrogenase reductase (NifH, Fe-protein) comprise the two-component complex metalloenzyme nitrogenase [1]. We present evidence suggesting that NifH/NifNE complex serves as the entry point for molybdenum into the FeMo-co biosynthetic pathway and that NifX may play a role in specifying the organic acid moiety of FeMo-co.
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