We have studied the growth on acetate, the metabolism of acetate enzymes, and respiration of a series of citrate synthase mutants of Saccharomyces cerevisiae. The results confirmed and extended our previous observation that cytosolic citrate synthase is not necessary for growth on acetate. Deletion of mitochondrial citrate synthase (CS1) protein resulted in changes in metabolites, decrease in t...

heterogeneous ziegler-natta and homogeneous metallocene catalysts exhibit greatly different active sitenature in olefin polymerization. in our previous study, it was reported that mgcl2-supported titanocenecatalysts can generate both ziegler-natta-type and metallocene-type active sites according to the type of activators.the dual active site nature of the supported titanocene catalysts was furt...

The ability of an enzyme to select and act upon a specific class of compounds with unerring precision and efficiency is an essential feature of life. Simultaneously, these enzymes often catalyze the reaction of a range of similar substrates of the same class, and also have promiscuous activities on unrelated substrates. Previously, we have established a methodology to quantify promiscuous activ...

The vibrational dynamics of water around glycine was investigated by using Raman spectroscopy and inelastic neutron scattering. Experiments of deuterated glycine versus deuterium were performed as comparison. The study shows that for glycine, the exchange of proton–deuteron on the active NH+3 side was easy, whereas there was hardly exchange on the CH2 side. Comparing different proportion of gly...

Heterogeneous Ziegler-Natta and homogeneous metallocene catalysts exhibit greatly different active sitenature in olefin polymerization. In our previous study, it was reported that MgCl2-supported titanocenecatalysts can generate both Ziegler-Natta-type and metallocene-type active sites according to the type of activators.The dual active site nature of the supported titanocene catalysts was furt...

Glycine acts as a necessary coagonist for glutamate at the NMDA receptor (NMDAR) complex by binding to the strychnine-insensitive glycine-B binding site on the NR1 subunit. The fact that glycine is normally found in the brain and spinal cord at concentrations that exceed those required to saturate this site has led to the speculation that glycine normally saturates NMDAR-containing synapses in ...