Speed and current control of permanent magnet synchronous motor drive using IMC controllers

The paper describes a current and speed control of the permanent magnet synchronous motor with vector control. For a current and speed controller, the Internal Model Control (IMC) method was chosen for its good tracking capability and demands on the controllers. A short analysis of the IMC method for design of the current and speed controller has been made. The paper contains mathematical description of the IMC controller design. Simulation and experimental results of the vector controlled AC drive with interior permanent magnet synchronous motor are shown to present features of the current and speed controller.Web of Science12410

Organometallic ruthenium anticancer complexes inhibit human glutathione-S-transferase π

The organometallic ruthenium(II) anticancer complexes [(η6- arene)Ru(en)Cl]+ (arene = p-cymene (1), biphenyl (2) or 9,10-dihydrophenanthrene (3); en = ethylenediamine), exhibit in vitro and in vivo anticancer activities. In the present work, we show that they inhibit human glutathione-S-transferase π (GSTπ) with IC50 values of 59.4 ± 1.3, 63.2 ± 0.4 and 37.2 ± 1.1 μM, respectively. Mass spectrometry revealed that complex 1 binds to the S-donors of Cys15, Cys48 within the G-site and Cys102 at the interface of the GSTπ dimer, while complex 2 binds to Cys48 and Met92 at the dimer interface and complex 3 to Cys15, Cys48 and Met92. Moreover, the binding of complex 1 to Cys15 and Cys102, complex 2 to Cys48 and complex 3 to Cys15 induces the irreversible oxidation of the coordinated thiolates to sulfenates. Molecular modeling studies indicate that the coordination of the {(arene)Ru(en)}2 + fragment to Cys48 blocks the hydrophilic G-site sterically, perhaps preventing substrate from proper positioning and accounting for the reduction in enzymatic activity of ruthenated GSTπ. The binding of the ruthenium arene complexes to Cys102 or Met92 disrupts the dimer interface which is an essential structural feature for the proper functioning of GSTπ, perhaps also contributing to the inhibition of GSTπ