| Abstrakt: |
Rubredoxin, a red nonheme iron protein previously shown to be an essential electron carrier in an enzyme system from Pseudomonas oleovoranswhich hydroxylates fatty acids and hydrocarbons, has been isolated in large quantities by an improved procedure. The protein is a single polypeptide chain with a molecular weight of 19,000 as determined by sedimentation studies and polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. It contains a single methionine residue and 10 cysteine residues and, unlike rubredoxins isolated from anaerobic bacteria, histidine and arginine. The isolated form of this protein, which contains 1 atom of iron and is called (1Fe)-rubredoxin, is readily converted to a form which contains 2 atoms of iron and is called (2Fe)-rubredoxin. |
