Purification and characterization of a molybdenum-pterin-binding protein (Mop) in Clostridium pasteurianum W5.
AUTOR(ES)
Hinton, S M
RESUMO
A large-scale fractionation scheme purified the major molybdenum(Mo)-binding protein (Mop) from crude extracts of Clostridium pasteurianum, with a 10 and 0.2% yield of Mo and protein, respectively. The apparent molecular weight of the purified molybdoprotein is 5,700, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The protein contains 0.7 mol of Mo per mol of protein with a molecular weight of 5,700. Mop, as isolated, has a peak absorbency at 293 nm. Denaturation and oxidation of the molybdoprotein released multiple pterin like fluorescent compounds. Mop appears to contain a pterin derivative and Mo, but phosphate analysis indicated that the pterin at the very least is not phosphorylated; phosphorylation is required for functional molybdenum cofactor. All treatments used to release the putative Mo-pterin species from Mop failed to yield a molybdopterin that had detectable molybdenum cofactor activity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=213536Documentos Relacionados
- Cloning, expression and sequencing the molybdenum-pterin binding protein (mop) gene of Clostridium pasteurianum in Escherichia coli.
- Characterization of Rhodobacter capsulatus genes encoding a molybdenum transport system and putative molybdenum-pterin-binding proteins.
- On the iron-sulfur cluster in hydrogenase from Clostridium pasteurianum W5.
- Role of molybdenum in dinitrogen fixation by Clostridium pasteurianum.
- Electron Paramagnetic Resonance of Nitrogenase and Nitrogenase Components from Clostridium pasteurianum W5 and Azotobacter vinelandii OP
