Molecular properties of high potential iron sulfur protein of Chromatium warmingii.
High potential iron sulfur protein (HIPIP) of the purple sulfur bacterium Chromatium warmingii was purified to homogeneity by ion exchange chromatography, gel filtration and ammonium sulfate fractionation. The acidic protein was isolated in the reduced form. The best purity index (A280/A388) obtained was 2.52, and 3.8 mumol of the protein was isolated out of 100 g wet cell material. The molecular weights estimated by sodium dodecylsulfate polyacrylamide gel electrophoresis and gel filtration through Sephacryl S-200 were 8900 and 10 500, respectively. The protein has an isoelectric point at pH 3.6 for the reduced form and at pH 3.8 for the oxidized form, and a midpoint redox potential of +355 mV. One mol of HIPIP contains 4 mol nonheme iron and 4 mol acid-labile sulfur.
D001426:Bacterial Proteins / Q000032:analysis* / Q000302:isolation & purification; D002841:Chromatiaceae / Q000032:analysis; D002844:Chromatium / Q000032:analysis*; D002850:Chromatography, Gel; D007506:Iron-Sulfur Proteins / Q000032:analysis* / Q000302:isolation & purification; D007526:Isoelectric Point; D008667:Metalloproteins / Q000032:analysis*; D008970:Molecular Weight; D045322:Photosynthetic Reaction Center Complex Proteins; D012241:Rhodopseudomonas / Q000032:analysis
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D045322:Photosynthetic Reaction Center Complex Proteins; C007943:high potential iron-sulfur protein