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- Pollmann, Stephan, et al. Show all 8 Authors
- Journal of the American Chemical Society 2016 v.138 no.24 pp. 7468-7471
- Methanocaldococcus; dissociation; electron paramagnetic resonance spectroscopy; methanogens; methionine; nitrogen; nitrogenase
- ... NifB utilizes two equivalents of S-adenosyl methionine (SAM) to insert a carbide atom and fuse two substrate [Fe–S] clusters forming the NifB cofactor (NifB-co), which is then passed to NifEN for further modification to form the iron–molybdenum cofactor (FeMo-co) of nitrogenase. Here, we demonstrate that NifB from the methanogen Methanocaldococcus infernus is a radical SAM enzyme able to reductive ...
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