The human obesity susceptibility gene, FTO, encodes a protein that is homologous to the DNA repair AlkB protein.The AlkB family proteins utilize iron(II), a-ketoglutarate (a-KG) and dioxygen to perform oxidative repair of alkylated nucleobases in DNA and RNA. We demonstrate here the oxidative demethylation of 3-methylthymine (3-meT) in singlestranded DNA (ssDNA) and 3-methyluracil (3-meU) in singlestranded RNA (ssRNA) by recombinant human FTO protein in vitro. Both human and mouse FTO proteins preferentially repair 3-meT in ssDNA over other base lesions tested. They showed negligible activities against 3-meT in double-stranded DNA (dsDNA). In addition, these two proteins can catalyze the demethylation of 3-meU in ssRNA with a slightly higher efficiency over that of 3-meT in ssDNA, suggesting that methylated RNAs are the preferred substrates for FTO.

A remarkable transformation to realize ortho arylation of acetanilides via Pd(II)-catalyzed C−H functionalization with trialkoxyarylsinaes was demonstrated.

No compass required: A method is described for forming biaryl CC bonds by a PdII‐catalyzed cross‐coupling of aryl CH bonds with aryl boronic acids under mild conditions without the presence of directing groups. Different substituents on both (hetero)arenes and aryl boronic acids are compatible with the reaction conditions, and the homocoupling of boronic acids is highly inhibited. Dioxygen was applied as the final oxidant.