Measurement of the tensor analyzing power T20 in the dd->^3Hen and dd->^3Hp at intermediate energies and at zero degree

The data on the tensor analyzing power T20 in the dd->^3Hen and dd-> ^3Hp reactions at 140, 200 and 270 MeV of the deuteron kinetic energy and at zero degree obtained at RIKEN Accelerator Research Facility are presented. The observed positive sign of T20 clearly demonstrates the sensitivity to the D/S wave ratios in the ^3He and ^3H in the energy domain of the measurements. The T20 data for the ^3He-n and ^3H-p channels are in agreement within experimental accuracy.Comment: 9 pages, 3 figures, submitted in Phys.Lett.

Reaction mechanism and characteristics of T_{20} in d + ^3He backward elastic scattering at intermediate energies

For backward elastic scattering of deuterons by ^3He, cross sections \sigma and tensor analyzing power T_{20} are measured at E_d=140-270 MeV. The data are analyzed by the PWIA and by the general formula which includes virtual excitations of other channels, with the assumption of the proton transfer from ^3He to the deuteron. Using ^3He wave functions calculated by the Faddeev equation, the PWIA describes global features of the experimental data, while the virtual excitation effects are important for quantitative fits to the T_{20} data. Theoretical predictions on T_{20}, K_y^y (polarization transfer coefficient) and C_{yy} (spin correlation coefficient) are provided up to GeV energies.Comment: REVTEX+epsfig, 17 pages including 6 eps figs, to be published in Phys. Rev.

Chemo-Mechanical Coupling in F1-ATPase Revealed by Catalytic Site Occupancy during Catalysis

F1-ATPase is a rotary molecular motor in which the central γ subunit rotates inside a cylinder made of α3β3 subunits. To clarify how ATP hydrolysis in three catalytic sites cooperate to drive rotation, we measured the site occupancy, the number of catalytic sites occupied by a nucleotide, while assessing the hydrolysis activity under identical conditions. The results show hitherto unsettled timings of ADP and phosphate releases: starting with ATP binding to a catalytic site at an ATP-waiting γ angle defined as 0°, phosphate is released at ∼200°, and ADP is released during quick rotation between 240° and 320° that is initiated by binding of a third ATP. The site occupancy remains two except for a brief moment after the ATP binding, but the third vacant site can bind a medium nucleotide weakly