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Soluble mouse CLK-1 (MCLK1) was expressed in Escherichia coli as a heterologous host to characterize the aging-associated enzyme CLK-1, which is proposed to be a member of the carboxylate-bridged diiron family of proteins. Biochemical analyses of the in vitro activity of MCLK1 with quinone substrates revealed that NADH could serve directly as a reductant for catalytic activation of dioxygen and substrate oxidation by the enzyme, in absence of an additional reductase protein component.

A facile synthesis of 2-carbamoyl-2-cyanocyclopropanecarboxylates through a tandem iodosobenzene/tetrabutylammonium iodide-induced oxidative cyclization and a subsequent neighboring group-assisted decarboxylation of the Michael adducts of 2-cyanoacetamides with [alpha],[beta]-unsaturated malonates is described. The method is observed to proceed smoothly under mild conditions and with good functional group tolerance and could be used to obtain highly functionalized cyclopropanes in moderate to good yields and with excellent diastereoselectivities.

The synthesis of analogues of the two reverse phosphonohydroxamic acids is described, in which the length of the carbon spacer is modified, the N-methyl group of the acid is replaced by an ethyl group and the phosphate group is replaced by isosteric moieties like sulfonate or carboxylate functionalities. The potential of the analogues to inhibit the Escherichia coli 1-deoxy-D-xylulose 5-phosphate reducto-isomerase (DXR) is analyzed.

The synthesis and structural characterization of a Ru(II) complex with a tetradentate ligand containing two carboxylate groups is reported. The newly isolated seven-coordinated Ru(IV) dimer complex containing a [HOHOH] bridging ligand during the process of catalytic water oxidation might provide new possibilities for the design of more efficient catalysts for water oxidation which is the key step for solar energy conversion into hydrogen by light-driven water splitting.

The isolation of a sulfate-reducing phenol-degrading bacterium, strain AK1, from a 2-bromophenol-utilizing sulfidogenic estuarine sediment enrichment culture and identification of a putative phenylphosphate synthase gene responsible for anaerobic phenol degradation in strain AK1 is reported. The results suggested that the pathway for anaerobic degradation of phenol in Desulfobacterium anilini strain AK1 proceeds via phosphorylation of phenol to phenylphosphate followed by carboxylation to 4-hydroxybenzoate.

The design and isolation of three new complexes in a system with six bonds and a distance of 6.9 Angstrom between the redox-active and basic sites is described. The small shift of the redox potential observed on protonation provides insight into decreased communication between the Ru and the carboxylate group compared to other system.