Article
The [4Fe-4S] cluster domain of the nitrogenase iron protein facilitates conformational changes required for the cooperative binding of two nucleotides.
Biochemistry - 10 Dec 1996
Ryle M J, Seefeldt L C
Abstract excerpt
MgATP binding and hydrolysis are central to all reduction reactions catalyzed by nitrogenase. The iron (Fe) protein component of nitrogenase is a homodimeric protein with a bridging [4Fe-4S] cluster and two nucleotide binding sites, one on each subunit. This work presents evidence that the [4Fe-4...
Topics
- Acetylene
- Adenosine Triphosphate
- Azotobacter vinelandii
- Circular Dichroism
- Electrochemistry
- Electron Spin Resonance Spectroscopy
- Ethylenes
- Iron-Sulfur Proteins
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Nitrogenase
- Nucleotides
- Oxidation-Reduction
- Protein Binding
- Protein Conformation
- Protein Structure, Secondary