Pub Date : 2024-07-11DOI: 10.3103/s0027131424700135
I. V. Grigoryan, V. V. Spiridonov, A. M. Adelyanov, Yu. A. Koksharov, K. V. Potapenkov, I. V. Taranov, G. B. Khomutov, A. A. Yaroslavov
Abstract
This paper presents new colloidal systems that have prospects for use as carriers of medicinal compounds and are polymer complexes based on polyacrylic acid molecules of various molecular weights and biogenic polyamine, additionally modified with magnetic iron oxide nanoparticles. The main physicochemical characteristics of the resulting polycomplexes are determined. The possibility of incorporating a doxorubicin medicinal compound in the polycomplexes is demonstrated, and the magnetic properties of the polycomplexes functionalized with magnetic iron oxide nanoparticles are studied.
{"title":"New Magnetic Colloidal Systems Based on Biomimetic Polycomplexes","authors":"I. V. Grigoryan, V. V. Spiridonov, A. M. Adelyanov, Yu. A. Koksharov, K. V. Potapenkov, I. V. Taranov, G. B. Khomutov, A. A. Yaroslavov","doi":"10.3103/s0027131424700135","DOIUrl":"https://doi.org/10.3103/s0027131424700135","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>This paper presents new colloidal systems that have prospects for use as carriers of medicinal compounds and are polymer complexes based on polyacrylic acid molecules of various molecular weights and biogenic polyamine, additionally modified with magnetic iron oxide nanoparticles. The main physicochemical characteristics of the resulting polycomplexes are determined. The possibility of incorporating a doxorubicin medicinal compound in the polycomplexes is demonstrated, and the magnetic properties of the polycomplexes functionalized with magnetic iron oxide nanoparticles are studied.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":null,"pages":null},"PeriodicalIF":0.7,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141614278","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-06-04DOI: 10.3103/s0027131424700019
O. V. Maslova, O. V. Senko, N. A. Stepanov, I. V. Lyagin, E. N. Efremenko
Abstract
Waste from the production and use of synthetic polymers is a serious problem. The development of enzymatic and microbial biocatalysts capable of degrading hard-to-decompose polymers seems to be one of the promising and environmentally oriented solutions to this problem. A possibility of combining biocatalysts (BCs)—enzymes and microbial cells—with metal catalysts is considered as a promising basis for the development of new hybrid chemobiocatalytic processes intended for the effective degradation of synthetic polymers (SPs).
{"title":"Biocatalysis in the Degradation of Synthetic Polymers","authors":"O. V. Maslova, O. V. Senko, N. A. Stepanov, I. V. Lyagin, E. N. Efremenko","doi":"10.3103/s0027131424700019","DOIUrl":"https://doi.org/10.3103/s0027131424700019","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>Waste from the production and use of synthetic polymers is a serious problem. The development of enzymatic and microbial biocatalysts capable of degrading hard-to-decompose polymers seems to be one of the promising and environmentally oriented solutions to this problem. A possibility of combining biocatalysts (BCs)—enzymes and microbial cells—with metal catalysts is considered as a promising basis for the development of new hybrid chemobiocatalytic processes intended for the effective degradation of synthetic polymers (SPs).</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":null,"pages":null},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141513810","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-06-04DOI: 10.3103/s0027131424700032
E. D. Belyaeva, N. V. Komarova, A. E. Kuznetsov
Abstract
Lactate oxidase is a practically important enzyme widely used to detect L-lactate in medical diagnostics and in the food industry. This review summarizes the results of protein engineering of lactate oxidases to clarify the underlying mechanism of action of the enzyme and to improve its performance properties.
{"title":"Protein Engineering of Lactate Oxidase","authors":"E. D. Belyaeva, N. V. Komarova, A. E. Kuznetsov","doi":"10.3103/s0027131424700032","DOIUrl":"https://doi.org/10.3103/s0027131424700032","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>Lactate oxidase is a practically important enzyme widely used to detect L-lactate in medical diagnostics and in the food industry. This review summarizes the results of protein engineering of lactate oxidases to clarify the underlying mechanism of action of the enzyme and to improve its performance properties.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":null,"pages":null},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141548878","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-06-04DOI: 10.3103/s0027131424700044
A. V. Endutkin, D. O. Zharkov
Abstract
DNA glycosylases are enzymes that hydrolyze the N-glycosidic bond of damaged nucleotides, initiating the process of base excision DNA repair. There are at least eight structural classes of these enzymes, differing in both their substrate specificity and the mechanism of catalysis. The review examines the mechanisms of human and bacterial DNA glycosylases that protect the genome from the major types of DNA damage.
摘要DNA糖基化酶是一种能水解受损核苷酸的N-糖苷键，启动碱基切除DNA修复过程的酶。这类酶至少有八种结构类别，它们在底物特异性和催化机制方面各不相同。本综述探讨了人类和细菌 DNA 糖基化酶的机制，这些酶保护基因组免受主要类型的 DNA 损伤。
{"title":"Strategies of N-Glycosidic Bond Cleavage by DNA Repair Enzymes","authors":"A. V. Endutkin, D. O. Zharkov","doi":"10.3103/s0027131424700044","DOIUrl":"https://doi.org/10.3103/s0027131424700044","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>DNA glycosylases are enzymes that hydrolyze the <i>N-</i>glycosidic bond of damaged nucleotides, initiating the process of base excision DNA repair. There are at least eight structural classes of these enzymes, differing in both their substrate specificity and the mechanism of catalysis. The review examines the mechanisms of human and bacterial DNA glycosylases that protect the genome from the major types of DNA damage.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":null,"pages":null},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141548875","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-06-04DOI: 10.3103/s002713142470007x
A. S. Cherkashina, O. O. Mikheeva, V. G. Akimkin
Abstract
This paper reviews the protein engineering of Bst polymerase using various methods. To modify the enzyme, approaches such as the production of chimeric proteins, directed evolution, and directed and random mutagenesis are used. Examples of successful changes in enzyme properties such as catalytic activity, processivity, thermal stability, and resistance to inhibitors are described.
{"title":"Protein Engineering of Bst Polymerase for Isothermal Amplification Purposes","authors":"A. S. Cherkashina, O. O. Mikheeva, V. G. Akimkin","doi":"10.3103/s002713142470007x","DOIUrl":"https://doi.org/10.3103/s002713142470007x","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>This paper reviews the protein engineering of Bst polymerase using various methods. To modify the enzyme, approaches such as the production of chimeric proteins, directed evolution, and directed and random mutagenesis are used. Examples of successful changes in enzyme properties such as catalytic activity, processivity, thermal stability, and resistance to inhibitors are described.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":null,"pages":null},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141548873","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-06-04DOI: 10.3103/s0027131424700081
D. M. Hushpulian, I. N. Gaisina, S. V. Nikulin, T. A. Chubar, S. S. Savin, I. G. Gazaryan, V. I. Tishkov
Abstract
World-wide introduction of high throughput screening (HTS) methods in drug discovery research did not result in the increased number of novel medications on the market. We discuss novel trends in drug discovery that came from the understanding that majority of diseases are multifactorial and that one enzyme has many protein substrates. Hence, new approaches are focused on development of drugs, which (1) trigger survival pathways to return the organism to homeostatic balance, and (2) inhibit enzymes modifying histones or transcription factors not at the active site, but by displacement of protein substrates from the enzyme complexes. A good example for both approaches comes from the development of activators of antioxidant defense. We analyze and illustrate problems of commonly used in vitro HTS assays, and briefly discuss advantages and limitations of small animal models. The novel approaches are complementary to the standard HTS and do not substitute for testing in mammals. Development of transgenic reporter mice to monitor drug effects by means of in vivo imaging is extremely promising to select proper dosage and administration regimes for full-range PK studies.
{"title":"High Throughput Screening in Drug Discovery: Problems and Solutions","authors":"D. M. Hushpulian, I. N. Gaisina, S. V. Nikulin, T. A. Chubar, S. S. Savin, I. G. Gazaryan, V. I. Tishkov","doi":"10.3103/s0027131424700081","DOIUrl":"https://doi.org/10.3103/s0027131424700081","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>World-wide introduction of high throughput screening (HTS) methods in drug discovery research did not result in the increased number of novel medications on the market. We discuss novel trends in drug discovery that came from the understanding that majority of diseases are multifactorial and that one enzyme has many protein substrates. Hence, new approaches are focused on development of drugs, which (1) trigger survival pathways to return the organism to homeostatic balance, and (2) inhibit enzymes modifying histones or transcription factors not at the active site, but by displacement of protein substrates from the enzyme complexes. A good example for both approaches comes from the development of activators of antioxidant defense. We analyze and illustrate problems of commonly used in vitro HTS assays, and briefly discuss advantages and limitations of small animal models. The novel approaches are complementary to the standard HTS and do not substitute for testing in mammals. Development of transgenic reporter mice to monitor drug effects by means of in vivo imaging is extremely promising to select proper dosage and administration regimes for full-range PK studies.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":null,"pages":null},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141548877","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-06-04DOI: 10.3103/s0027131424700020
A. M. Rozhkova, Yu. A. Denisenko, I. G. Sinelnikov, I. N. Zorov, D. V. Erokhin, V. G. Dzhavakhia
Abstract
Expression of recombinant proteins is important for studying their biological functions. For the primary description of protein properties, the E. coli expression system is most often used. However, in overexpression conditions, the rate of aggregation of target proteins often exceeds the rate of proper folding, resulting in the formation of insoluble inclusion bodies. Inclusion bodies are a clear disadvantage of the E. coli expression system since they prevent the extraction of target recombinant proteins. The use of chaperone-like proteins in vitro while refolding a target protein is one of the solutions to the existing problem. In this study, the MF3 recombinant protein is an example of a chaperone-like protein, which increases the yield of soluble plant chitinase by 92% compared to the yield of this protein using the standard refolding procedure.
{"title":"Application of MF3 Microbial Recombinant Protein in Refolding of Plant Chitinase","authors":"A. M. Rozhkova, Yu. A. Denisenko, I. G. Sinelnikov, I. N. Zorov, D. V. Erokhin, V. G. Dzhavakhia","doi":"10.3103/s0027131424700020","DOIUrl":"https://doi.org/10.3103/s0027131424700020","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>Expression of recombinant proteins is important for studying their biological functions. For the primary description of protein properties, the <i>E. coli</i> expression system is most often used. However, in overexpression conditions, the rate of aggregation of target proteins often exceeds the rate of proper folding, resulting in the formation of insoluble inclusion bodies. Inclusion bodies are a clear disadvantage of the <i>E. coli</i> expression system since they prevent the extraction of target recombinant proteins. The use of chaperone-like proteins in vitro while refolding a target protein is one of the solutions to the existing problem. In this study, the MF3 recombinant protein is an example of a chaperone-like protein, which increases the yield of soluble plant chitinase by 92% compared to the yield of this protein using the standard refolding procedure.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":null,"pages":null},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141513809","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-06-04DOI: 10.3103/s0027131424700093
M. G. Khrenova, T. I. Mulashkina, A. M. Kulakova, I. V. Polyakov, A. V. Nemukhin
Abstract
The combined quantum mechanics/molecular mechanics method is most often used to describe the molecular mechanisms of enzymatic reactions. The review discusses the main methodological issues, gives practical recommendations, and also illustrates the progress of the method over the past 20 years using an important example of the reaction of guanosine triphosphate hydrolysis by a protein complex.
{"title":"Computer Modeling of the Mechanisms of Enzymatic Reactions: Lessons from 20 Years of Practice","authors":"M. G. Khrenova, T. I. Mulashkina, A. M. Kulakova, I. V. Polyakov, A. V. Nemukhin","doi":"10.3103/s0027131424700093","DOIUrl":"https://doi.org/10.3103/s0027131424700093","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>The combined quantum mechanics/molecular mechanics method is most often used to describe the molecular mechanisms of enzymatic reactions. The review discusses the main methodological issues, gives practical recommendations, and also illustrates the progress of the method over the past 20 years using an important example of the reaction of guanosine triphosphate hydrolysis by a protein complex.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":null,"pages":null},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141548872","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-06-04DOI: 10.3103/s0027131424700068
D. I. Bagaeva, G. R. Demina, M. O. Agaphonov, A. P. Savitsky, A. S. Kaprelyants, M. O. Shleeva
Abstract
The transition of active Mycolicibacterium smegmatis cells to a dormant state under acidification conditions is accompanied by the intracellular accumulation of tetramethyl ester of coproporphyrin (TMC). At the same time, the dormant forms of mycobacteria develop resistance to a number of damaging factors. The addition of 5-aminolevulinic acid (ALA), a precursor of porphyrin synthesis, into the bacterial culture medium leads to the accumulation of TMC in actively growing cells, which simulates the situation with dormant mycobacteria. Upon threefold increasing the concentration of TMC, the bacteria become sevenfold more resistant to the action of 40 mM hydrogen peroxide and 90-fold more resistant to heating up to 80°C. At the same time, in M. smegmatis cells with an increased concentration of TMC, the activity of dichlorophenolindophenol reductase that is a marker of respiratory chain activity decreases by 18%. The detected inhibition of activity can lead to a decrease in side oxidative reactions in the cell. Therefore, the accumulation of methylated coproporphyrin is possibly one of the mechanisms for the development of mycobacterium resistance at dormancy.
{"title":"Methylation of Coproporphyrin as a Protective Mechanism in Mycobacteria under Adverse Conditions","authors":"D. I. Bagaeva, G. R. Demina, M. O. Agaphonov, A. P. Savitsky, A. S. Kaprelyants, M. O. Shleeva","doi":"10.3103/s0027131424700068","DOIUrl":"https://doi.org/10.3103/s0027131424700068","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>The transition of active <i>Mycolicibacterium smegmatis</i> cells to a dormant state under acidification conditions is accompanied by the intracellular accumulation of tetramethyl ester of coproporphyrin (TMC). At the same time, the dormant forms of mycobacteria develop resistance to a number of damaging factors. The addition of 5-aminolevulinic acid (ALA), a precursor of porphyrin synthesis, into the bacterial culture medium leads to the accumulation of TMC in actively growing cells, which simulates the situation with dormant mycobacteria. Upon threefold increasing the concentration of TMC, the bacteria become sevenfold more resistant to the action of 40 mM hydrogen peroxide and 90-fold more resistant to heating up to 80°C. At the same time, in <i>M. smegmatis</i> cells with an increased concentration of TMC, the activity of dichlorophenolindophenol reductase that is a marker of respiratory chain activity decreases by 18%. The detected inhibition of activity can lead to a decrease in side oxidative reactions in the cell. Therefore, the accumulation of methylated coproporphyrin is possibly one of the mechanisms for the development of mycobacterium resistance at dormancy.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":null,"pages":null},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141548876","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2024-06-04DOI: 10.3103/s0027131424700056
V. I. Muronetz, M. V. Medvedeva, E. V. Schmalhausen
Abstract
The main types of oxidative post-translational modifications of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDН) targeting the sulfhydryl group of the catalytic cysteine residue Cys152 are reviewed. The highly reactive sulfhydryl group of Cys152 in the active center of GAPDH undergoes oxidation and S-nitrosylation, leading to inactivation and destabilization of the enzyme. Upon reversible oxidation of the sulfhydryl group to form cysteine-sulfenic acid, the enzyme loses dehydrogenase activity, but gains the ability to catalyze the acyl-phosphatase reaction. Hydrolysis of the product of the dehydrogenase reaction, 1,3-diphosphoglycerate, under the action of oxidized GAPDH leads to uncoupling of oxidation and phosphorylation at this stage of glycolysis. The action of nitric oxide results in S-nitrosylation of Cys152 in GAPDH with the subsequent formation of cysteine-sulfenic acid due to hydrolysis of the S-NO-group. Data are presented on the relationship between S-nitrosylation, oxidation and S-glutathionylation of Cys152 in GAPDH. The role of post-translational modifications of the sulfhydryl group of the catalytic cysteine residue in the regulation of enzyme activity, as well as the mechanisms ensuring the reversibility of such modifications are discussed.
{"title":"Post-Translational Modifications of the Sulfhydryl Group of the Cysteine Residue of Glyceraldehyde-3-phosphate Dehydrogenase","authors":"V. I. Muronetz, M. V. Medvedeva, E. V. Schmalhausen","doi":"10.3103/s0027131424700056","DOIUrl":"https://doi.org/10.3103/s0027131424700056","url":null,"abstract":"<h3 data-test=\"abstract-sub-heading\">Abstract</h3><p>The main types of oxidative post-translational modifications of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDН) targeting the sulfhydryl group of the catalytic cysteine residue Cys152 are reviewed. The highly reactive sulfhydryl group of Cys152 in the active center of GAPDH undergoes oxidation and <i>S</i>-nitrosylation, leading to inactivation and destabilization of the enzyme. Upon reversible oxidation of the sulfhydryl group to form cysteine-sulfenic acid, the enzyme loses dehydrogenase activity, but gains the ability to catalyze the acyl-phosphatase reaction. Hydrolysis of the product of the dehydrogenase reaction, 1,3-diphosphoglycerate, under the action of oxidized GAPDH leads to uncoupling of oxidation and phosphorylation at this stage of glycolysis. The action of nitric oxide results in <i>S</i>-nitrosylation of Cys152 in GAPDH with the subsequent formation of cysteine-sulfenic acid due to hydrolysis of the S-NO-group. Data are presented on the relationship between <i>S</i>-nitrosylation, oxidation and <i>S</i>-glutathionylation of Cys152 in GAPDH. The role of post-translational modifications of the sulfhydryl group of the catalytic cysteine residue in the regulation of enzyme activity, as well as the mechanisms ensuring the reversibility of such modifications are discussed.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":null,"pages":null},"PeriodicalIF":0.7,"publicationDate":"2024-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141548874","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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