Substrate Interaction at an Iron-Sulfur Face of the FeMo-cofactor during Nitrogenase Catalysis

This publication has 34 references indexed in Scilit:

• Localization of a Catalytic Intermediate Bound to the FeMo-cofactor of Nitrogenase
  Journal of Biological Chemistry, 2004
• Binding Sites of Nitrogenase: Kinetic and Theoretical Studies of Cyanide Binding to Extracted FeMo-Cofactor Derivatives
  Inorganic Chemistry, 2003
• Localization of a Substrate Binding Site on the FeMo-Cofactor in Nitrogenase: Trapping Propargyl Alcohol with an α-70-Substituted MoFe Protein
  Biochemistry, 2003
• Reduction of short chain alkynes by a nitrogenase α-70Ala-substituted MoFe proteinBased on the presentation given at Dalton Discussion No. 4, 10–13th January 2002, Kloster Banz, Germany. Research supported by National Institutes of Health Grant R01-GM59087.
  J. Chem. Soc., Dalton Trans., 2002
• Interaction of Acetylene and Cyanide with the Resting State of Nitrogenase α-96-Substituted MoFe Proteins
  Biochemistry, 2001
• Differential Effects on N₂ Binding and Reduction, HD Formation, and Azide Reduction with α-195^His- and α-191^Gln-Substituted MoFe Proteins of Azotobacter vinelandii Nitrogenase
  Biochemistry, 2000
• Spectroscopic Evidence for Changes in the Redox State of the Nitrogenase P-Cluster during Turnover
  Biochemistry, 1999
• Role of the MoFe Protein .alpha.-Subunit Histidine-195 Residue in FeMo-cofactor Binding and Nitrogenase Catalysis
  Biochemistry, 1995
• X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-.ANG. resolution
  Biochemistry, 1993
• Biological nitrogen fixation by way of an enzyme-bound dinitrogen-hydride intermediate
  Nature, 1978