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Vacuolar (H(+))-ATPases, also called V-ATPases, are ATP-driven proton pumps that are highly phylogenetically conserved. Early biochemical and cell biological studies have revealed many details of the molecular mechanism of proton pumping and of the structure of the multi-subunit membrane complex, including the stoichiometry of subunit composition. In addition, yeast and mouse genetics have broadened our understanding of the physiological consequences of defective vacuolar acidification and its related disease etiologies. Recently, phenotypic investigation of V-ATPase mutants in Caenorhabditis elegans has revealed unexpected new roles of V-ATPases in both cellular function and early development. In this review, we discuss the functions of the V-ATPases discovered in C. elegans.

An efficient transition-metal-free intermolecular benzylic amidation with sulfonamides is described. Various valuable nitrogen-containing compounds, including amines, beta-chloro amine, amino alcohol, alpha-, beta-amino ester, and N-sulfonyl imine, are generated from the preferential N-functionalization of saturated benzylic C-H bonds. The potential of this reaction system also lies in the fact it can be developed into an environmentally friendly intermolecular amidation process.

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