Metal and sulfur composition of iron-molybdenum cofactor of nitrogenase.
AUTOR(ES)
Nelson, M J
RESUMO
The sulfur content of N-methylformamide solutions of cofactor from Clostridium pasteurianum nitrogenase has been determined to be 11.9 (+/- 0.9) mol per mol of molybdenum. This number was determined radiochemically, using iron-molybdenum cofactor isolated from molybdenum-iron protein from bacteria grown on 35SO4. A total of 3.2 (+/- 0.2) mol of sulfur per mol of molybdenum was found to be present in cysteine and methionine, probably arising from contaminating proteins not intrinsic to the cofactor. Combined with accumulated evidence that is discussed, these results lead to an updated stoichiometry of MoFe6S8 or 9, not MoFe6S4 as previously thought, for this cluster.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=393327Documentos Relacionados
- Plausible structure of the iron-molybdenum cofactor of nitrogenase.
- Biosynthesis of iron-molybdenum cofactor in the absence of nitrogenase.
- In vitro synthesis of the iron-molybdenum cofactor of nitrogenase.
- Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase.
- Isolation of an iron-molybdenum cofactor from nitrogenase*