In vitro synthesis of the iron-molybdenum cofactor of nitrogenase.
AUTOR(ES)
Shah, V K
RESUMO
Molybdate- and ATP-dependent in vitro synthesis of the iron-molybdenum cofactor (FeMo-co) of nitrogenase requires the protein products of at least the nifB, nifN, and nifE genes. Extracts of FeMo-co-negative mutants of Klebsiella pneumoniae and Azotobacter vinelandii with lesions in different genes can be complemented for FeMo-co synthesis. Both K. pneumoniae and A. vinelandii dinitrogenase (component I) deficient in FeMo-co can be activated by FeMo-co synthesized in vitro. Properties of the partially purified dinitrogenase activated by FeMo-co synthesized in vitro were comparable to those of dinitrogenase from the wild-type organism; e.g., ratios of acetylene- to nitrogen-reduction activities, as well as those of acetylene reduction activities to EPR spectrum peak height at g = 3.65, were very similar. A. vinelandii mutants UW45 and CA30 have mutations in a gene functionally equivalent to nifB of K. pneumoniae.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=323138Documentos Relacionados
- Plausible structure of the iron-molybdenum cofactor of nitrogenase.
- Biosynthesis of iron-molybdenum cofactor in the absence of nitrogenase.
- Metal and sulfur composition of iron-molybdenum cofactor of nitrogenase.
- nifV-dependent, low-molecular-weight factor required for in vitro synthesis of iron-molybdenum cofactor of nitrogenase.
- Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase.