Publications by authors named "R R Davydov"

Introduction: Pathology of the nose and paranasal sinuses currently occupy one of the leading places in the general structure of diseases of the ENT organs. The proportion of patients in this group who are treated in highly specialized departments of the hospital and who undergo surgical interventions in the nasal cavity is more than 65%.

Objective: To equalize the efficacy and safetyof the preparation Sinupret in combination with standard therapy in patients in the preoperative and postoperative periods with planned surgical interventions in violation of the architectonics of the nasal cavity.

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Nowadays, with the increase in the rhythm of life, the relevance of using express diagnostics methods for human health state estimation has significantly increased. We present a new express diagnostics method based on non-invasive measurements (the pulse wave shape, heart rate, blood pressure, and oxygen saturation of blood vessels and tissues). A feature of these measurements is that they can be carried out both in the hospital and at home.

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In this report, we investigate the physical and chemical properties of monocopper Cu(I) superoxo and Cu(II) peroxo and hydroperoxo complexes. These are prepared by cryoreduction/annealing of the parent [LCu(O)] Cu(I) dioxygen adducts with the tripodal, N-coordinating, tetradentate ligands L = tmpa, tmpa, TMGtren and are best described as [LCu(O)] Cu(II) complexes that possess end-on (η-O) superoxo coordination. Cryogenic γ-irradiation (77 K) of the EPR-silent parent complexes generates mobile electrons from the solvent that reduce the [LCu(O)] within the frozen matrix, trapping the reduced form fixed in the structure of the parent complex.

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Efficiently carrying out the oxygen reduction reaction (ORR) is critical for many applications in biology and chemistry, such as bioenergetics and fuel cells, respectively. In biology, this reaction is carried out by large, transmembrane oxidases such as heme-copper oxidases (HCOs) and cytochrome oxidases. Common to these oxidases is the presence of a glutamate residue next to the active site, but its precise role in regulating the oxidase activity remains unclear.

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The electron configuration of flavin cofactors, FMN and FAD, is a critical factor governing the reactivity of NADPH-cytochrome P450 reductase (CPR). The current view of electron transfer by the mammalian CPR, based on equilibrium redox potentials of the flavin cofactors, is that the two electron-reduced FMN hydroquinone (FMNH2), rather than one electron-reduced FMN semiquinone, serves as electron donor to the terminal protein acceptors. However, kinetic and thermodynamic studies on the CPR species originated from different organisms have shown that redox potentials measured at distinct electron transfer steps differ from redox potentials determined by equilibrium titration.

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