[Purification and properties of phototrophic bacteria Thiocapsa roseopersicina hydrogenase bound with chromatophores].
The method of solution and puridication of hydrogenase from chromatophores of purpur sulphur bacteria Thiocapsa roseopersicina strain BBS are described. Hydrogenase molecular weight is 73000. It contains 4,4 mole S2- and 3.1 mole Fe2+ per mole of protein; pI 4.15. The enzyme absorption spectrum has the maximun et 400-410 nm, which is characteristic of proteins containing non-haem iron. Membrane--linked enzyme as well as soluble hydrogenase of that microorganism is characterized by high thermal stability: inactivation occurs at the temperature above 78 degrees C when the optimal temperature for that enzyme is 70 degrees C. Homogenous enzyme catalyses D2--H2O exchange reaction, reversible redox reaction of methyl viologene and benzyl viologene.
D020130:Bacterial Chromatophores / Q000201:enzymology*; D002841:Chromatiaceae / Q000201:enzymology*; D004355:Drug Stability; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000032:analysis; D008566:Membranes / Q000201:enzymology; D008970:Molecular Weight; D010088:Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D011485:Protein Binding; D013455:Sulfur / Q000032:analysis; D014755:Viologens / Q000378:metabolism
D014755:Viologens; D013455:Sulfur; D007501:Iron; D010088:Oxidoreductases
Ochistka i svoĭstva sviazannoĭ s khromatoforami gidrogenazy fototrofnoĭ bakterii Thiocapsa roseopersicina