Identification of a nitrogenase FeMo cofactor precursor on NifEN complex
AUTOR(ES)
Hu, Yilin
FONTE
National Academy of Sciences
RESUMO
The biosynthesis of the FeMo cofactor (FeMoco) of Azotobacter vinelandii nitrogenase presumably starts with the production of its Fe/S core by NifB (the nifB gene product). This core is subsequently processed on the α2β2 tetrameric NifEN complex (formed by the nifE and nifN gene products). In this article, we identify a NifEN-bound FeMoco precursor form that can be converted to fully assembled FeMoco in a so-called FeMoco-maturation assay containing only purified components. We also establish that only molybdate, homocitrate, MgATP, and Fe protein are essential for FeMoco maturation. The FeMoco-maturation assay described here will further address the remaining questions related to the assembly mechanism of the ever-intriguing FeMoco.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=552928Documentos Relacionados
- N coordination of FeMo cofactor requires His-195 of the MoFe protein alpha subunit and is essential for biological nitrogen fixation.
- Desenvolvimento e caracterização de um banho nãocianetado para a eletrodeposição de ligas de Fe-Mo : caracterização dos filmes de Fe-Mo
- Electrodeposition of Ni-Mo and Fe-Mo alloys from sulfate-citrate acid solutions
- Structure-function relationships in the alpha subunit of Klebsiella pneumoniae nitrogenase MoFe protein from analysis of nifD mutants.
- Nucleotide and deduced amino acid sequences of nifD encoding the alpha-subunit of nitrogenase MoFe protein of Clostridium pasteurianum.
