[High potential iron-sulfur protein from Thiocapsa roseopersicina].
A high potential protein (HiPIP) containing a [4Fe-4S] cluster was obtained in a homogeneous state from the purple sulfur bacterium T. roseopersicina strain BBS. The EPR and absorption spectra are specific for this type of proteins. In the absorption spectrum the A283/A390 ratio equals to 2.25; Mr = 10 000, pI is 4.08, E0' = +328 mV. The reduced form of HiPIP was found to be more stable upon storage; T 1/2 is 40 min at 80 degrees C. HiPIP can be reduced by ascorbate, cysteine, 2-mercaptoethanol and sulfide as well as by formate, H2 and NADPH in the presence of corresponding enzymes. Chromatophores oxidize HiPIP in the light. This suggests that the latter takes part in the photosynthetic electron transfer chain of T. roseopersicina.
D002844:Chromatium / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000302:isolation & purification* / Q000378:metabolism; D008667:Metalloproteins / Q000302:isolation & purification*; D008970:Molecular Weight; D011199:Potentiometry; D013056:Spectrophotometry, Ultraviolet
D007506:Iron-Sulfur Proteins; D008667:Metalloproteins
Vysokopotentsial'nyĭ zhelezosernyĭ belok Thiocapsa roseopersicina.