OAT (organic anion transporter) 2 [human gene symbol SLC22A7 (SLC is solute carrier)] is a member of the SLC22 family of transport proteins. In the rat, the principal site of expression of OAT2 is the sinusoidal membrane domain of hepatocytes. The particular physiological function of OAT2 in liver has been unresolved so far. In the present paper, we have used the strategy of LC (liquid chromato...

Metal catalysis has a dominant role in modern organic chemistry. In particular, crosscoupling reactions allow bond formations, which have previously been impossible to perform.[1] Precious metal catalysts dominate the field, but alternative systems based on nickel and copper salts have also, historically, been important. In particular, recent systems based on these metals have been described th...

The 5,10-methenyltetrahydrofolate (5,10-CH=H4folate) synthetase catalyses the physiologically irreversible formation of 5,10-CH=H4folate from 5-formyltetrahydrofolate (5-HCO-H4folate) and ATP. It is not clear how (or if) 5-HCO-H4folate is formed in vivo. Using a spectrophotometric assay for 5-HCO-H4folate, human recombinant 5,10-CH=H4folate cyclohydrolase, which catalyses the hydrolysis of 5,10...

An enzyme preparation that catalyses the deacylation of monoand di-acyl phospholipids, galactosyl diglycerides, monoand di-glycerides has been partially purified from potato tubers. The preparation also hydrolyses methyl and pnitrophenyl esters and acts preferentially on esters of long-chain fatty acids. Triglycerides, wax esters and sterol esters are not hydrolysed. The same enzyme preparation...

The copper complex Tp(CF3)2,BrCu(NCMe) efficiently catalyses the aziridination of olefins in water using PhI=NTs as nitrene source, with identical activity than that observed when dichloromethane solvent, under same experimental conditions. No specific modification catalyst or substrates are required, nor presence additional phase transfer catalyst. Competition experiments and Hammett plots sho...

Riboflavin synthase catalyses a mechanistically complex dismutation affording riboflavin and 5-amino-6-ribitylamino-2,4(1H,3H )-pyrimidinedione from 6,7-dimethyl-8-ribityllumazine. A pentacyclic adduct (compound 2 ) of two substrate molecules was used as substrate for pre-steady-state kinetic analysis. Whereas the wild-type enzyme catalyses the decomposition of compound 2 into a mixture of ribo...

1. Dihydroxyfumarate slowly autoxidizes at pH6. This reaction is inhibited by superoxide dismutase but not by EDTA. Mn2+ catalyses dihydroxyfumarate oxidation by reacting with O2 leads to to form Mn3+, which seems to oxidize dihydrofumarate rapidly. Cu2+ also catalyses dihydroxyfumarate oxidation, but by a mechanism that does not involve O2 leads to. 2. Peroxidase catalyses oxidation of dihydro...

A [bis(imino)pyridine-iron(II)] complex efficiently catalyses the oxidation of C(sp3)-H bonds by dihydrogen peroxide, through the attack of the alkyl substrate by hydroxyl radicals.

A Cu-diamine complex effectively catalyses tandem C-N bond formation on 2-(2-haloalkenyl)-aryl halide substrates, to deliver a series of N-functionalised indoles. Anilines, amides and carbamates are all effective coupling partners under the developed conditions.