A ruthenium-based biomimetic hydrogen cluster for efficient photocatalytic hydrogen generation from formic acid.

A ruthenium-based biomimetic hydrogen cluster, [Ru2 (CO)6 (µ-SCH2 CH2 CH2 S)] (1), has been synthesized and, in the presence of the P ligand tri(o-tolyl)phosphine, demonstrated efficient photocatalytic hydrogen generation from formic acid decomposition. Turnover frequencies (TOFs) of 5500 h(-1) and turnover numbers (TONs) over 24 700 were obtained with less than 50 ppm of the catalyst, thus representing the highest TOFs for ruthenium complexes as well as the best efficiency for photocatalytic hydrogen production from formic acid. Moreover, 1 showed high stability with no significant degradation of the photocatalyst observed after prolonged photoirradiation at 90 °C.

Inductive properties of polypyridyl ruthenium complexes significantly regulate various protein distributions in Escherichia coli.

Ruthenium complexes with similar octahedral structures but different intrinsic inductive properties significantly influence the total cellular protein distributions, which may affect different metabolic pathways. A systematic study of the relationship between ruthenium complexes and Escherichia coli was undertaken, using two-dimensional gel electrophoresis analysis and the identification of various proteins by mass data mining. Based on the low similarities (<40%) between the total protein distributions, the inductive properties of the ruthenium complexes are relevant to the formation of the protein-Ru interaction in addition to the Ru-DNA interaction. Two major protein functions in E. coli BL21 that were reduced by compound 1 were oxidoreductases and transporters, corresponding to 29% and 25% of the 24 down-regulated proteins. The main biological processes of the proteins down-regulated by compound 1 were related to carbohydrate reactions, including in transport, tricarboxylic acid (TCA) cycle, glycolysis, and gluconeogenesis. All four ruthenium complexes shared similar up-regulated proteins, including clpB and kpyk1, and down-regulated similar proteins, including ompA and ybbN. This result supports that the presence of Ru-protein interactions is a major factor affecting bacteria growth, and particularly transport and carbohydrate-related reactions.