Article
Secretion of both partially unfolded and folded apoproteins of dimethyl sulfoxide reductase by spheroplasts from a molybdenum cofactor-deficient mutant of Rhodobacter sphaeroides f. sp. denitrificans.
Journal of bacteriology - 1 Mar 1994
Masui H, Satoh M, Satoh T
Abstract excerpt
Spheroplasts prepared from a molybdenum cofactor-deficient mutant of Rhodobacter sphaeroides f. sp. denitrificans secreted dimethyl sulfoxide (DMSO) reductase which had no molybdenum cofactor and therefore no activity, whereas those from wild-type cells secreted the active reductase. The inactive...
Topics
- Apoenzymes
- Chromatography, Gel
- Coenzymes
- Electrophoresis, Polyacrylamide Gel
- Iron-Sulfur Proteins
- Metalloproteins
- Molybdenum Cofactors
- Mutation
- Oxidoreductases
- Protein Conformation
- Pteridines
- Rhodobacter sphaeroides
- Spheroplasts
- Trypsin
- Urea