A S Utada | PubMed Health

PubMed2005

Monodisperse double emulsions generated from a microcapillary device.

Double emulsions are highly structured fluids consisting of emulsion drops that contain smaller droplets inside. Although double emulsions are potentially of commercial value, traditional fabrication by means of two emulsification steps leads to very ill-controlled structuring. Using a microcapillary device, we fabricated double emulsions that contained a single internal droplet in a core-shell geometry. We show that the droplet size can be quantitatively predicted from the flow profiles of the fluids. The double emulsions were used to generate encapsulation structures by manipulating the properties of the fluid that makes up the shell. The high degree of control afforded by this method and the completely separate fluid streams make this a flexible and promising technique.

Journal Article↗

PubMed2001

Interaction of the substrate radical and the 5'-deoxyadenosine-5'-methyl group in vitamin B(12) coenzyme-dependent ethanolamine deaminase.

The distance and relative orientation of the C5' methyl group of 5'-deoxyadenosine and the substrate radical in vitamin B(12) coenzyme-dependent ethanolamine deaminase from Salmonella typhimurium have been characterized by using X-band two-pulse electron spin-echo envelope modulation (ESEEM) spectroscopy in the disordered solid state. The (S)-2-aminopropanol-generated substrate radical catalytic intermediate was prepared by cryotrapping steady-state mixtures of enzyme in which catalytically exchangeable hydrogen sites in the active site had been labeled by previous turnover on (2)H(4)-ethanolamine. Simulation of the time- and frequency-domain ESEEM requires two types of coupled (2)H. The strongly coupled (2)H has an effective dipole distance (r(eff)) of 2.2 A, and isotropic coupling constant (A(iso)) of -0.35 MHz. The weakly coupled (2)H has r(eff) = 3.8 A and A(iso) = 0 MHz. The best (2)H ESEEM time- and frequency-domain simulations are achieved with a model in which the hyperfine couplings arise from one strongly coupled hydrogen site and two equivalent weakly coupled hydrogen sites located on the C5' methyl group of 5'-deoxyadenosine. This model indicates that the unpaired electron on C1 of the substrate radical and C5' are separated by 3.2 A and are thus at closest contact. The close proximity of C1 and C5' indicates that C5' of the 5'-deoxyadenosyl moiety directly mediates radical migration between cobalt in cobalamin and the substrate/product site over a distance of 5-7 A in the active site of ethanolamine deaminase.

Binding Sites↗