Article
Systematic mutations of highly conserved His49 and carboxyl-terminal of recombinant porcine liver NADH-cytochrome b5 reductase solubilized domain.
Biochimica et biophysica acta - 19 Mar 1999
Kimura S, Emi Y, Ikushiro S, Iyanagi T
Abstract excerpt
The cDNA encoding solubilized porcine liver NADH-cytochrome b5 reductase catalytic domain (Pb5R) was cloned and overexpressed in Escherichia coli. A highly conserved His49 and a C-terminal Phe272 of Pb5R, which are located near the isoalloxazine moiety of the FAD, were systematically modulated by site-directed mutagenesis. Large structural change was not detected on the absorption and circular dichroism spectra...
Topics
- Amino Acid Sequence
- Animals
- Base Sequence
- Circular Dichroism
- Cytochrome Reductases
- Cytochrome-B(5) Reductase
- DNA, Complementary
- Escherichia coli
- Histidine
- Liver
- Molecular Sequence Data
- Mutation
- Oxidation-Reduction
- Protein Structure, Tertiary
- Recombinant Proteins
- Solubility
- Swine