Article
Characterization of a nif-regulated flavoprotein (FprA) from Rhodobacter capsulatus. Redox properties and molecular interaction with a [2Fe-2S] ferredoxin.
European journal of biochemistry - 1 Feb 2000
Jouanneau Y, Meyer C, Asso M, Guigliarelli B, Willison J C
Abstract excerpt
A flavoprotein from Rhodobacter capsulatus was purified as a recombinant (His)6-tag fusion from an Escherichia coli clone over-expressing the fprA structural gene. The FprA protein is a homodimer containing one molecule of FMN per 48-kDa monomer. Reduction of the flavoprotein by dithionite showed biphasic kinetics, starting with a fast step of semiquinone (SQ) formation, and followed by a slow reduction of the...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Base Sequence
- Cross-Linking Reagents
- DNA Primers
- Escherichia coli
- Ferredoxins
- Flavoproteins
- Gene Deletion
- Gene Expression
- Genes, Bacterial
- Kinetics
- Nitrogen Fixation
- Oxidation-Reduction