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Alternative NADH dehydrogenases (NADH:ubiquinone oxidoreductases) are single subunit respiratory chain enzymes found in plant and fungal mitochondria and in many bacteria. It is unclear how these peripheral membrane proteins interact with their hydrophobic substrate ubiquinone. Known inhibitors of alternative NADH dehydrogenases bind with rather low affinities. We have identified 1-hydroxy-2-dodecyl-4(1H)quinolone as a high affinity inhibitor of alternative NADH dehydrogenase from Yarrowia lipolytica. Using this compound, we have analyzed the bisubstrate and inhibition kinetics for NADH and decylubiquinone. We found that the kinetics of alternative NADH dehydrogenase follow a ping-pong mechanism. This suggests that NADH and the ubiquinone headgroup interact with the same binding pocket in an alternating fashion.
We calculate thermal photon and neutral pion spectra in ultrarelativistic heavy-ion collisions in the framework of three-fluid hydrodynamics. Both spectra are quite sensitive to the equation of state used. In particular, within our model, recent data for S + Au at 200 AGeV can only be understood if a scenario with a phase transition (possibly to a quark-gluon plasma) is assumed. Results for Au+Au at 11 AGeV and Pb + Pb at 160 AGeV are also presented.