42 research outputs found
Catalyst activation by loss of cyclopentadienyl ligands in hydrogen transfer catalysis with Cp*IrIII complexes
The activity of the two related complexes [Cp*Ir(IMe) 2X]BF4 (X = Cl (1), H (2)) in transfer hydrogenation from isopropyl alcohol to acetophenone was investigated. The results suggest that the commonly accepted monohydride mechanism for transfer hydrogenation mediated by cyclopentadienyl iridium species does not apply to chloride 1. We have found evidence that, although the two monodentate NHC ligands are retained in the coordination sphere, the Cp* ligand is completely released under mild conditions in a precatalytic activation step. Synthesis of modified versions of the initial precatalyst 1 with different cyclopentadienyl and NHC ligands demonstrated that increasing the steric pressure around the iridium center facilitates precatalyst activation and thus enhances the catalytic performance. Study of five new iridium(III) complexes bearing mono- or diphosphines helped us monitor Cp* ligand loss under mild conditions. An unusual P-C bond cleavage was also noted in a 1,2-bis(dimethylphosphino)methane (dmpm) ligand. On the basis of these findings, a novel catalyst activation mechanism is proposed for [(η5-C5R5)Ir] transfer hydrogenation based on the lability of the cyclopentadienyl ligand. © 2014 American Chemical Society
Electrochemical activation of cp∗ iridium complexes for electrode-driven water-oxidation catalysis
Operando Structure Activity Stability Relationship of Iridium Oxides during the Oxygen Evolution Reaction
Creating active and stable electrodes is an essential step toward efficient and durable electrolyzers. To achieve this goal, understanding what aspects of the electrode structure dictate activity and catalyst dissolution is key. Here, we investigate these aspects by studying trends in the activity, stability, and operando structure of iridium oxides during the oxygen evolution reaction. Using operando X-ray photoelectron and X-ray absorption spectroscopy, we determined the near-surface structure of oxides ranging from amorphous to crystalline during the reaction. We show that applying oxygen evolution potentials universally yields deprotonated μ2-O moieties and a μ1-O/μ1-OH mixture, with universal deprotonation energetics but in different amounts. This quantitative difference mainly results from variations in deprotonation depth: surface deprotonation for crystalline IrO2 versus near-surface deprotonation for semicrystalline and amorphous IrOx. We argue that both surface deprotonation and subsurface deprotonation modify the barrier for the oxygen evolution and Ir dissolution reactions, thus playing an important role in catalyst performance
Physiological and biochemical adaptations to training in Rana pipiens
Fifteen Rana pipiens were trained on a treadmill thrice weekly for 6.5 weeks to assess the effects of training on an animal that supports activity primarily through anaerobiosis. Endurance for activity increased 35% in these frogs as a result of training ( P =0.006, Fig. 1). This increased performance was not due to enhanced anaerobiosis. Total lactate produced during exercise did not differ significantly for the trained or untrained animals in either gastrocnemius muscle (2.77±0.21 and 2.82±0.13 mg/g, respectively) or whole body (1.32±0.10 and 1.47±0.06 mg/g, respectively). Glycogen depletion also did not differ between the two groups (Fig. 2c). The primary response to training appeared to involve augmentation of aerobic metabolism, a response similar to that reported for mammals. Gastrocnemius muscles of trained frogs underwent a 38% increase over those of untrained individuals in the maximum activity of citrate synthase (14.5±1.0 and 10.5±0.9 μmoles/(g wet wt·min); P =0.008). This enzyme was also positively correlated with the level of maximum performance for all animals tested ( r =0.61, P <0.01) and with the degree of improvement in the trained animals ( r =0.72, P <0.05). In addition to an increased aerobic capacity, the trained animals demonstrated a greater removal of lactate from the muscle 15 min after fatigue (Fig. 2b).Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/47124/1/360_2004_Article_BF00710002.pd