Identification of a nitrogenase protein-protein interaction site defined by residues 59 through 67 within the Azotobacter vinelandii Fe protein.
Peters, J W
Identification of a nitrogenase protein-protein interaction site defined by residues 59 through 67 within the Azotobacter vinelandii Fe protein. [electronic resource] - The Journal of biological chemistry Nov 1994 - 28076-83 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
0021-9258
Adenosine Triphosphate--metabolism
Amino Acid Sequence
Azotobacter vinelandii--enzymology
Base Sequence
Binding Sites
Cloning, Molecular
Clostridium--enzymology
Escherichia coli
Genes, Bacterial
Kinetics
Molecular Sequence Data
Molybdoferredoxin--metabolism
Mutagenesis, Site-Directed
Nitrogenase--biosynthesis
Oligodeoxyribonucleotides
Oxidoreductases
Protein Conformation
Identification of a nitrogenase protein-protein interaction site defined by residues 59 through 67 within the Azotobacter vinelandii Fe protein. [electronic resource] - The Journal of biological chemistry Nov 1994 - 28076-83 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
0021-9258
Adenosine Triphosphate--metabolism
Amino Acid Sequence
Azotobacter vinelandii--enzymology
Base Sequence
Binding Sites
Cloning, Molecular
Clostridium--enzymology
Escherichia coli
Genes, Bacterial
Kinetics
Molecular Sequence Data
Molybdoferredoxin--metabolism
Mutagenesis, Site-Directed
Nitrogenase--biosynthesis
Oligodeoxyribonucleotides
Oxidoreductases
Protein Conformation