Quantum coherence of the molecular states and their corresponding currents in nanoscale Aharonov-Bohm interferometers

By considering a nanoscale Aharonov-Bohm (AB) interferometer containing a parrallel-coupled double dot coupled to the source and drain electrodes, we investigate the AB phase oscillations of transport current via the bonding and antibonding state channels. The results we obtained justify the experimental analysis given in [Phys. Rev. Lett. \textbf{106}, 076801 (2011)] that bonding state currents in different energy configurations are almost the same. On the other hand, we extend the analysis to the transient transport current components flowing through different channels, to explore the effect of the parity of bonding and antibonding states on the AB phase dependence of the corresponding current components in the transient regime. The relations of the AB phase dependence between the quantum states and the associated current components are analyzed in details, which provides useful information for the reconstruction of quantum states through the measurement of the transport current in such systems. With the coherent properties in the quantum dot states as well as in the transport currents, we also provide a way to manipulate the bonding and antibonding states by the AB magnetic flux.Comment: 10 pages, 7 figure

Improvement of activity and stability of chloroperoxidase by chemical modification

<p>Abstract</p> <p>Background</p> <p>Enzymes show relative instability in solvents or at elevated temperature and lower activity in organic solvent than in water. These limit the industrial applications of enzymes.</p> <p>Results</p> <p>In order to improve the activity and stability of chloroperoxidase, chloroperoxidase was modified by citraconic anhydride, maleic anhydride or phthalic anhydride. The catalytic activities, thermostabilities and organic solvent tolerances of native and modified enzymes were compared. In aqueous buffer, modified chloroperoxidases showed similar <it>K</it>_mvalues and greater catalytic efficiencies <it>k</it>_cat/<it>K</it>_mfor both sulfoxidation and oxidation of phenol compared to native chloroperoxidase. Of these modified chloroperoxidases, citraconic anhydride-modified chloroperoxidase showed the greatest catalytic efficiency in aqueous buffer. These modifications of chloroperoxidase increased their catalytic efficiencies for sulfoxidation by 12%~26% and catalytic efficiencies for phenol oxidation by 7%~53% in aqueous buffer. However, in organic solvent (DMF), modified chloroperoxidases had lower <it>K</it>_mvalues and higher catalytic efficiencies <it>k</it>_cat/<it>K</it>_mthan native chloroperoxidase. These modifications also improved their thermostabilities by 1~2-fold and solvent tolerances of DMF. CD studies show that these modifications did not change the secondary structure of chloroperoxidase. Fluorescence spectra proved that these modifications changed the environment of tryptophan.</p> <p>Conclusion</p> <p>Chemical modification of epsilon-amino groups of lysine residues of chloroperoxidase using citraconic anhydride, maleic anhydride or phthalic anhydride is a simple and powerful method to enhance catalytic properties of enzyme. The improvements of the activity and stability of chloroperoxidase are related to side chain reorientations of aromatics upon both modifications.</p