title: [Purification and properties of hydrogenase from phototrophic bacterium Thiocapsa roseopersicina].
abstract: The isolation method and some peoperties of purple sulphur bacteria (Thiocapsa roseopersicina strain BBS) hydrogenase are described Hydrogenase molecular weight is found to be 66000; it contains 3.7 moles of S2- and 3.9 moles of Fe2+ per one mole of the enzyme;pI=4.2. The enzyme absorption spectrum has the maximum at 400-412 nm which is characteristic of proteins containing non-haem iron. Hydrogenase is suggested to consist pf 4 subunits of two types: with molar weight 27000 and 6000. Unlike other hydrogenases, this enzyme is rather resistant to O2 and is more thermostable: the inactivation of the enzyme was observed at the temperature above 80 degrees C; Hydrogenase preparation catalyses D2-H2O exchange reaction, H2 evolution from the reduced methyl viologene (MV) and H2 absorption in the presense of MV or benzylviologene but not in the presense of NAD(P), FAD, FMN, azocarmine, methylene blue and ferricyanide.
mesh_terms: D002841:Chromatiaceae / Q000201:enzymology*; D002849:Chromatography, Gas; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007501:Iron / Q000032:analysis; D008970:Molecular Weight; D010088:Oxidoreductases / Q000032:analysis* / Q000302:isolation & purification; D013455:Sulfur / Q000032:analysis
chemical_list: D013455:Sulfur; D007501:Iron; D010088:Oxidoreductases
vernacular_title: Ochistka i svoĭstva godrogenazy iz fototrofnoĭ bakterii Thiocapsa roseopersicina