Stereochemistry and chiroptical properties of bimetallic single helicates of hexapyrrole-α, ω-dicarbaldimines with high diastereoselectivity

Bimetallic complexes of hexapyrrole-[Formula: see text],[Formula: see text]-dicarbaldimines consisting of a pair of four-coordinate metal sites adopt a helical closed [Formula: see text]-symmetric form or sigmoidal open forms depending on whether the 2,2[Formula: see text]-bipyrrole subunit at the center of the hexapyrrole chain takes cis- or trans-conformation. X-ray crystallography of a bisNi complex having N-[([Formula: see text]-1-cyclohexylethyl]carbaldimine units at both ends of the hexapyrrole chain revealed a non-symmetric heterohelical open form where the metal coordination sites of opposite helical sense sit on opposite sides of the central 2,2[Formula: see text]-bipyrrole subunit. BisPd complexes preferred a closed [Formula: see text] form and a steric bulk at the 3,3[Formula: see text]-position of the 2,2[Formula: see text]-bipyrrole subunit improved the helical sense bias. A bisPd complex with N-[([Formula: see text]-1-cyclohexylethyl]carbaldimine units adopts a helical closed [Formula: see text] form exclusively with full bias for a [Formula: see text]-helical sense. These bimetallic single stranded helicates were reversibly oxidized to [Formula: see text]-cation radicals at 0.1[Formula: see text]0.3 V vs. a ferrocene/ferrocenium couple and spectroelectrochemistry revealed remarkable absorption and CD spectral changes in the Vis-NIR region.

Moodle e-course management system as a tool for holding distance Olympiads at university

The article reveals the functionality of the e-courses management system Moodle as a tool for holding Olympiads in a distance format. The technology of development of tasks for the Olympiad is described, taking into account their implementation in Moodle, and two ways of presenting tasks are shown: 1) as a single test with a given number of questions and with different forms of test questions; 2) in the form of several separate tests, distributed over course modules. It is substantiated that the choice of the way of presenting tasks depends on the specifics of the Olympiad and on the presence/absence of the need to divide tasks into thematic modules. A description of the types of test questions that can be used for the tasks of the Olympiad is given: open form, closed form, multiple choice, essays, etc. As an example, the stages of developing an Olympiad in information security for students of pedagogical university are described. The system of tasks of the Olympiad is given and it is shown how to present these tasks in Moodle for automatic and manual checking. The technology described in the article allows the development of distance Olympiads for both students and schoolchildren. Students of pedagogical university were selected as the target audience. The procedure for evaluating the Olympiad tasks completed by students in manual and automated form is demonstrated with specific examples.

Structural analysis and reaction mechanism oaf malate dehydrogenase from Geobacillus stearothermophilus

Malate dehydrogenase (MDH) catalyzes the reversible reduction of oxaloacetate (OAA) to L-malate using nicotinamide adenine dinucleotide hydrogen. MDH has two characteristic loops, the mobile loop and the catalytic loop, in the active site. On binding to the substrate, the enzyme undergoes a structural change from the open-form, with an open conformation of the mobile loop, to the closed-form, with the loop in a closed conformation. In this study, three crystals of MDH from a moderate thermophile, Geobacillus stearothermophilus (gs-MDH) were used to determine four different enzyme structures (resolutions, 1.95–2.20 Å), each of which was correspondingly assigned to its four catalytic states. Two OAA-unbound structures exhibited the open-form, while the other two OAA-bound structures exhibited both the open- and closed-form. The structural analysis suggested that the binding of OAA to the open-form gs-MDH promotes conformational change in the mobile loop and simultaneously activates the catalytic loop. The mutations on the key amino acid residues involving the proposed catalytic mechanism significantly affected the gs-MDH activity, supporting our hypothesis. These findings contribute to the elucidation of the detailed molecular mechanism underlying the substrate recognition and structural switching during the MDH catalytic cycle.

A conformational switch driven by phosphorylation regulates the activity of the evolutionarily conserved SNARE Ykt6

Ykt6 is a soluble N-ethylmaleimide sensitive factor activating protein receptor (SNARE) critically involved in diverse vesicular fusion pathways. While most SNAREs rely on transmembrane domains for their activity, Ykt6 dynamically cycles between the cytosol and membrane-bound compartments where it is active. The mechanism that regulates these transitions and allows Ykt6 to achieve specificity toward vesicular pathways is unknown. Using a Parkinson’s disease (PD) model, we found that Ykt6 is phosphorylated at an evolutionarily conserved site which is regulated by Ca2+ signaling. Through a multidisciplinary approach, we show that phosphorylation triggers a conformational change that allows Ykt6 to switch from a closed cytosolic to an open membrane-bound form. In the phosphorylated open form, the spectrum of protein interactions changes, leading to defects in both the secretory and autophagy pathways, enhancing toxicity in PD models. Our studies reveal a mechanism by which Ykt6 conformation and activity are regulated with potential implications for PD.