Article
Isolation and characterization of nitrogenase MoFe protein from the mutant strain pHK17 of Klebsiella pneumoniae in which the two bridging cysteine residues of the P-clusters are replaced by the non-coordinating amino acid alanine.
The Biochemical journal - 15 Aug 1996
Yousafzai F K, Buck M, Smith B E
Abstract excerpt
Nitrogenase MoFe protein (Kp1) from the mutant strain pHK17 or Klebsiella pneumoniae has been purified to give three catalytically active fractions. In this mutant, each of the two bridging cysteine ligands to the P-clusters, alpha-Cys-89 and beta-Cys-94, has been replaced by a non-coordinating r...
Topics
- Adenosine Triphosphate
- Alanine
- Catalysis
- Disulfides
- Electron Spin Resonance Spectroscopy
- Hydrogen-Ion Concentration
- Iron
- Klebsiella pneumoniae
- Molybdenum
- Molybdoferredoxin
- Mutation
- Nitrogenase
- Oxidation-Reduction
- Protein Conformation
- Substrate Specificity