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1.
Phys Rev Lett ; 104(7): 075001, 2010 Feb 19.
Article in English | MEDLINE | ID: mdl-20366892

ABSTRACT

New features of instabilities driven by energetic ions are revealed. It is found that these instabilities can affect plasma heating and rotation by channeling the energy and momentum of the energetic ions to the region where the destabilized waves are damped. Because of the energy channeling, the plasma core may not be heated by the energetic ions even when these ions have a very peaked radial distribution. It is likely that this new phenomenon can explain experiments on the spherical torus NSTX where a broadening of the temperature profile and even a drop of the temperature at the plasma center with increasing injected power were observed during Alfvén instabilities [D. Stutman, Phys. Rev. Lett. 102, 115002 (2009)10.1103/PhysRevLett.102.115002]. The momentum channeling can lead to plasma rotation and frequency chirping due to the Doppler shift varying in time.

2.
Phys Rev Lett ; 94(16): 165004, 2005 Apr 29.
Article in English | MEDLINE | ID: mdl-15904237

ABSTRACT

Enhanced plasma heat conductivity in the presence of kinetic Alfvén waves (KAW) is predicted theoretically. The enhancement is shown to be strongest when the electron collision frequency exceeds the particle transit frequency in the wave field. Alfvén waves (both KAW and ideal MHD Alfvén eigenmodes generating the KAW) are studied in a shot of the Wendelstein 7-AS stellarator. On the basis of these results, strong thermal crashes observed during bursting Alfvénic activity in the mentioned shot are explained.

3.
Ukr Biokhim Zh (1978) ; 65(1): 97-100, 1993.
Article in Russian | MEDLINE | ID: mdl-8351750

ABSTRACT

Quinones inactivate oxidized glutathione reductase (EC 1.6.4.2) from yeast with rate constants (ki) ranging from 0.03 M-1s-1 (p-benzoquinone) to 10(3) M-1s-1 (bromanyl). It is glutathione, but not NADP+ that protects the enzyme from inactivation, which shows that quinones interact with a glutathione-binding centre, cysteine-2, most probably. The mechanism of inactivation by quinones differs from that by nitrosoureas which inactivate only the reduced enzyme, modifying the reduced catalytic disulphide. 1,3-bis-(2-chloroethyl)-1-nitrosourea acts as the most rapid inactivator of the enzyme, possessing ki of 0.77 M-1s-1.


Subject(s)
Glutathione Reductase/antagonists & inhibitors , Nitrosourea Compounds/pharmacology , Quinones/pharmacology , Binding Sites/drug effects , Catalysis , Kinetics , Molecular Structure , Oxidation-Reduction , Saccharomyces cerevisiae/enzymology
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