13 research outputs found
Π€ΠΈΠ·ΠΈΠΊΠΎ-Ρ ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΎΡΠ½ΠΎΠ²Ρ Ρ ΠΈΠΌΠΈΠΈ ΠΈ ΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΠΈ ΠΏΠ»Π°ΡΠΈΠ½ΠΎΠ²ΡΡ ΠΌΠ΅ΡΠ°Π»Π»ΠΎΠ² ΠΈ ΠΈΡ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΠΉ
The date of investigation on chemistry and technology of platinum metals in the large years are presented. The complexes of palladium(II) with macroheterocyclyc compounds are syntesited. The application of electrochemical processes for selection of platinum metals from solutions and applyed of concentrate of platinum metals is shownΠΡΠ°ΡΠΊΠΎ ΡΠ°ΡΡΠΌΠΎΡΡΠ΅Π½Ρ ΡΠ΅Π·ΡΠ»ΡΡΠ°ΡΡ Π²ΡΠΏΠΎΠ»Π½Π΅Π½Π½ΡΡ
Π² ΠΏΠΎΡΠ»Π΅Π΄Π½ΠΈΠ΅ Π³ΠΎΠ΄Ρ ΡΠ°Π±ΠΎΡ Π² ΠΎΠ±Π»Π°ΡΡΠΈ Ρ
ΠΈΠΌΠΈΠΈ ΠΈ ΡΠ΅Ρ
Π½ΠΎΠ»ΠΎΠ³ΠΈΠΈ ΠΏΠ»Π°ΡΠΈΠ½ΠΎΠ²ΡΡ
ΠΌΠ΅ΡΠ°Π»Π»ΠΎΠ². ΠΡΠΏΠΎΠ»Π½Π΅Π½ ΡΠΈΠ½ΡΠ΅Π· ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠΎΠ² ΠΏΠ°Π»Π»Π°Π΄ΠΈΡ(II) Ρ ΠΌΠ°ΠΊΡΠΎΠ³Π΅ΡΠ΅ΡΠΎΡΠΈΠΊΠ»ΠΈΡΠ΅ΡΠΊΠΈΠΌΠΈ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅-Π½ΠΈΡΠΌΠΈ. ΠΠΎΠΊΠ°Π·Π°Π½Π° Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΠΎΡΡΡ ΠΏΡΠΈΠΌΠ΅Π½Π΅Π½ΠΈΡ ΡΠ»Π΅ΠΊΡΡΠΎΡ
ΠΈΠΌΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΠΌΠ΅ΡΠΎΠ΄Π° Π΄Π»Ρ ΠΈΠ·Π²Π»Π΅ΡΠ΅Π½ΠΈΡ ΠΏΠ»Π°ΡΠΈΠ½ΠΎΠ²ΡΡ
ΠΌΠ΅ΡΠ°Π»Π»ΠΎΠ² ΠΈΠ· ΡΠ°ΡΡΠ²ΠΎΡΠΎΠ² ΠΈ ΠΏΠΎΠ»ΡΡΠ΅Π½ΠΈΡ ΠΊΠΎΠ½ΡΠ΅Π½ΡΡΠ°ΡΠΎΠ²
The physico-chemical results of chemistry and technology of platinum metals and their compounds
The date of investigation on chemistry and technology of platinum metals in the large years are presented. The complexes of palladium(II) with macroheterocyclyc compounds are syntesited. The application of electrochemical processes for selection of platinum metals from solutions and applyed of concentrate of platinum metals is show
Reversible inhibition of Escherichia coli inorganic pyrophosphatase by fluoride: trapped catalytic intermediates in cryo-crystallographic studies
Here, we describe high-resolution X-ray structures of Escherichia coli inorganic pyrophosphatase (E-PPase) complexed with the substrate, magnesium, or manganese pyrophosphate. The structures correspond to steps in the catalytic synthesis of enzyme-bound pyrophosphate (PP(i)) in the presence of fluoride as an inhibitor of hydrolysis. The catalytic reaction intermediates were trapped applying a new method that we developed for initiating hydrolytic activity in the E-PPase crystal. X-ray structures were obtained for three consecutive states of the enzyme in the course of hydrolysis. Comparative analysis of these structures showed that the Mn2+-supported hydrolysis of the phosphoanhydride bond is followed by a fast release of the leaving phosphate from the P1 site. The electrophilic phosphate P2 is trapped in the "down" conformation. Its movement into the "up" position most likely represents the rate-limiting step of Mn2+-supported hydrolysis. We further determined the crystal structure of the Arg43Gln mutant variant of E-PPase complexed with one phosphate and four Mn ions