Article
Nitrogenase-catalyzed ethane production and CO-sensitive hydrogen evolution from MoFe proteins having amino acid substitutions in an alpha-subunit FeMo cofactor-binding domain.
The Journal of biological chemistry - 5 Oct 1992
Scott D J, Dean D R, Newton W E
Abstract excerpt
Unlike wild type, certain Mo-dependent nitrogenases, which are expressed in non-N2-fixing mutant strains of Azotobacter vinelandii and have single amino acid substitutions within a region of the MoFe protein alpha-subunit proposed to encompass an FeMo cofactor-binding domain, are able to catalyze the reduction of acetylene by both two and four electrons to yield ethylene and ethane, respectively (Scott, D. J.,...
Topics
- Amino Acids
- Azotobacter vinelandii
- Carbon Monoxide
- Catalysis
- Electron Spin Resonance Spectroscopy
- Ethane
- Hydrogen
- Molybdoferredoxin
- Mutation
- Nitrogenase
- Temperature