Journal of Biological Inorganic Chemistry最新文献

{"title":"Critical evaluation of two neutron structures of Mn superoxide dismutase with quantum refinement","authors":"Kristoffer J. M. Lundgren,&nbsp;Justin Bergmann,&nbsp;Esko Oksanen,&nbsp;Ulf Ryde","doi":"10.1007/s00775-026-02140-5","DOIUrl":"10.1007/s00775-026-02140-5","url":null,"abstract":"<div>\u0000 \u0000 <p>In 2021, neutron structures of oxidised and reduced human manganese superoxide dismutase were published, suggesting several unexpected features, including deprotonated glutamate, tyrosine and histidine residues and a reduced Mn ion with two hydroxide ligands. We have used quantum refinement to evaluate whether alternative interpretations of the structures are possible, comparing many structural models with different possible protonation states or other structural interpretations. Quantum refinement is standard crystallographic refinement in which the empirical restraints, which are employed to ensure that the structure makes chemical sense and gives reasonable bond lengths and angles, are replaced by quantum mechanical calculations for a small but interesting part of the structure. We show that in all cases, there are more chemically reasonable interpretations of the structures, not involving any deprotonated residues, which give slightly improved structures in terms of real-space Z scores based on the difference maps and strain energies. Weak nuclear densities do not necessarily indicate that an atom is not present; instead it may indicate that the atom may have several conformations or shows extensive dynamics. For the Tyr-34 residue, our results indicate that the phenolic hydroxide H atom should preferably be within the aromatic ring plane (by ~20 kJ/mol), but with two possible conformations. Moreover, an Mn-bound water molecule can readily accept a hydrogen bond from the nearby Gln-143 residue.</p>\u0000 </div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 on","pages":"173 - 191"},"PeriodicalIF":2.8,"publicationDate":"2026-03-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-026-02140-5.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147430059","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Emerging role of mitoNEET as mitochondrial sensor of hypoxia","authors":"Nghi Thao Hoang,&nbsp;Kourosh Honarmand Ebrahimi","doi":"10.1007/s00775-026-02139-y","DOIUrl":"10.1007/s00775-026-02139-y","url":null,"abstract":"<div>\u0000 \u0000 <p>Mitochondria are organelles whose function and dynamics, that is fission, fusion, transport and selective removal (mitophagy), are fundamental for eukaryotic cells. Their dysfunction is associated with age-related neurodegeneration and the aging immune system. MitoNEET, an iron-sulfur (Fe-S) cluster-containing protein localised at the outer membrane of mitochondria, has emerged as a key regulator of mitochondrial respiration and linked to fission, fusion, and mitophagy. In this perspective article, we discuss recent emerging evidence describing the mitoNEET [2Fe-2S] cluster role as a sensor of the cellular level of O₂. These findings provide a mechanistic explanation of how mitochondria sense hypoxia, which affects their bioelectrochemistry and dynamics. We hope our data and analysis stimulate future research to fully understand the chemistry and biology of this intriguing Fe-S protein. These studies are expected to reveal new mechanistic insight into mitochondrial function and dynamics and help develop new therapeutics for inflammatory and age-related diseases.</p>\u0000 <span>AbstractSection</span>\u0000 Graphical Abstract\u0000 <div><figure><div><div><picture><source><img></source></picture></div></div></figure></div>\u0000 \u0000 </div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 on","pages":"119 - 130"},"PeriodicalIF":2.8,"publicationDate":"2026-03-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-026-02139-y.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147389031","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Study of the interaction of ferrocenium salts with oligonucleotide by CVA, UV-visible and CD-spectroscopy","authors":"Ludmila N. Telegina,&nbsp;Anastasia S. Sipieva,&nbsp;Daria A. Utepova,&nbsp;Alexey N. Rodionov,&nbsp;Alexander A. Simenel","doi":"10.1007/s00775-026-02138-z","DOIUrl":"10.1007/s00775-026-02138-z","url":null,"abstract":"<div>\u0000 \u0000 <p>The complexation of ferrocenium salts (with various anions) with an oligonucleotide (CCACGAGCTCCCACATGGT, <b>OL</b>) was studied using a combination of electrochemical (CVA) and spectral (UV-<i>vis</i> and CD spectroscopy) methods. It has been shown that varying the nature of the counteranion has virtually no effect on the binding constant to ferrocenium. However, the counterion can alter the secondary structure of the oligonucleotide, which may open a way to tune the biological activity of the ferrocenium cation.</p>\u0000 </div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 4","pages":"293 - 301"},"PeriodicalIF":2.8,"publicationDate":"2026-03-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147388950","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization and biological evaluation of a Rh(III) complex featuring Phosphonate-Modified bipyridine ligands","authors":"Thamilarasan Vijayan,&nbsp;Atifa Ashraf,&nbsp;Mohammad Azam,&nbsp;Jinheung Kim","doi":"10.1007/s00775-026-02135-2","DOIUrl":"10.1007/s00775-026-02135-2","url":null,"abstract":"<div>\u0000 \u0000 <p>A cyclopentadienyl rhodium(III) complex incorporating a phosphonate-functionalized 2,2′-bipyridine ligand was synthesized and comprehensively characterized to elucidate its biomolecular interactions and biological activity. The complex was structurally confirmed by spectroscopic and analytical techniques and further investigated using density functional theory (DFT) calculations to evaluate its electronic structure and frontier molecular orbitals. The interaction of the Rh(III) complex with calf thymus DNA was systematically examined using UV–visible absorption, fluorescence displacement assays with ethidium bromide, circular dichroism spectroscopy, and viscosity measurements. The results indicate a strong affinity toward DNA with an intrinsic binding constant of 2.85 × 10⁴ M⁻¹, consistent with a non-classical binding mode dominated by groove association rather than full intercalation. Molecular docking studies support this conclusion, revealing preferential minor-groove binding stabilized by hydrogen bonding and electrostatic interactions between the cationic metal center and the DNA phosphate backbone. Protein binding studies with bovine serum albumin (BSA) were carried out using absorption and fluorescence quenching experiments, demonstrating static quenching behavior and strong binding affinity, consistent with a single-site interaction. In vitro cytotoxicity assays revealed that the Rh(III) complex exhibits significant antiproliferative activity against MDA-MB-231 and A549 cancer cell lines, while displaying minimal toxicity toward normal VERO cells. Fluorescence microscopy using AO/EB staining confirmed apoptosis as the predominant mode of cell death. In addition, the complex showed pronounced antibacterial and antifungal activity against both Gram-positive and Gram-negative microorganisms. Overall, this study highlights the utility of phosphonate-modified Cp*Rh(III) complexes as multifunctional bioactive platforms, integrating detailed analytical characterization, theoretical insight, and biological evaluation, and provides a framework for the rational design of metal-based agents with tunable biomolecular interactions.</p>\u0000 <span>AbstractSection</span>\u0000 Graphical Abstract\u0000 <div><figure><div><div><picture><source><img></source></picture><span>The alternative text for this image may have been generated using AI.</span></div></div></figure></div>\u0000 \u0000 </div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 1-2","pages":"77 - 89"},"PeriodicalIF":2.7,"publicationDate":"2026-02-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146155479","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Meso-fluorinated cobalamins: insights into synthesis and redox properties","authors":"Ilia A. Dereven’kov,&nbsp;Vladimir S. Osokin,&nbsp;Ilya A. Khodov","doi":"10.1007/s00775-026-02133-4","DOIUrl":"10.1007/s00775-026-02133-4","url":null,"abstract":"<div><p>Here, we present the first method of synthesis of cyano- (F-CNCbl) and aqua (F-H₂OCbl) cobalamins, fluorinated at the C10 (<i>meso</i>) position of the corrin ring, and characterization of their redox properties. The reductive decyanation of F-CNCbl by glutathione and the reduction of F-H₂OCbl to Co(II)-form (F-Cbl(II)) by glutathione or reduced nicotinamide adenine dinucleotide proceed more efficiently than the reactions involving unmodified complexes, which may facilitate their intracellular processing, especially in the case of patients with impaired metabolism of CblC-protein. The stability of the C-F bond in fluorinated Cbls displays remarkable stability upon F-Cbl(II) reduction to the Co(I) form is a remarkable finding, in stark contrast to the elimination of the Br atom in meso-brominated cobalamin is eliminated during this process.</p><h3>Graphical Abstract</h3><div><figure><div><div><picture><source><img></source></picture><span>The alternative text for this image may have been generated using AI.</span></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 1-2","pages":"65 - 75"},"PeriodicalIF":2.7,"publicationDate":"2026-02-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146103585","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A bezafibrate bearing Pt(IV) prodrug triggers ferroptosis via modulating lipid metabolism in lung cancer cells","authors":"Neng Wan,&nbsp;Xuan-Lin Ren,&nbsp;Xiang-Yu Ma,&nbsp;Tao Zhu,&nbsp;Cheng-Zhi Xie,&nbsp;Jing-Yuan Xu,&nbsp;Xin Qiao","doi":"10.1007/s00775-025-02132-x","DOIUrl":"10.1007/s00775-025-02132-x","url":null,"abstract":"<div>\u0000 \u0000 <p>Ferroptosis, a unique modality of regulated cell death, is intricately intertwined with lipid peroxidation, a process tightly regulated by lipid metabolism. Herein, a Pt(IV) prodrug, CB, <i>cis</i>,<i> cis</i>,<i> trans</i>-[Pt(NH₃)₂Cl₂(BEZ)(OH)] (BEZ = bezafibrate), previously designed by conjugating the clinical platinum drug cisplatin with the lipid-modulating agent bezafibrate, exhibited potent anticancer efficacy via a unique mechanism of action independent of peroxisome proliferator-activated receptor α (PPARα) activation. Oil Red O staining and ultra-high-performance liquid chromatography-mass spectrometry (UPLC-MS) analysis revealed that CB reduced the total lipid content and altered the free fatty acid (FFA) profile in A549 cells. This alteration led to a reduction in both saturated fatty acids (SFA) and monounsaturated fatty acids (MUFA), while concurrently enhancing the proportion of polyunsaturated fatty acids (PUFA) to MUFA ratio. This change in lipid composition enhances the susceptibility of the cell membrane to lipid peroxidation, thereby triggering the ferroptosis. The antiproliferative effect of CB was partially reversed by the ferroptosis inhibitor, ferrostatin-1, confirming the involvement of ferroptosis. Mechanistically, CB induces lipid peroxidation, disrupts iron homeostasis (elevated Fe²⁺), and impairs redox balance (decreased GSH and increased MDA). Western blot analysis revealed that CB inhibits the Xc⁻/GSH/GPX4 antioxidant system and modulates iron pathway proteins. This multifaceted mechanism, which combines lipid modulation, ferroptosis induction, and DNA damage, highlights the potential of targeting lipid metabolism in cancer therapy.</p>\u0000 <span>AbstractSection</span>\u0000 Graphical abstract\u0000 <p>Pt(IV) prodrug, CB, a combination of cisplatin and bezafibrate, acts via a multifaceted anticancer mechanism including lipid-modulating, ferroptosis induction, apoptosis induction and DNA damage.</p><div><figure><div><div><picture><source><img></source></picture><span>The alternative text for this image may have been generated using AI.</span></div></div></figure></div>\u0000 \u0000 </div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 1-2","pages":"49 - 64"},"PeriodicalIF":2.7,"publicationDate":"2026-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146008532","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Making connections: teaching and learning bioelectrochemistry","authors":"James P. McEvoy","doi":"10.1007/s00775-025-02131-y","DOIUrl":"10.1007/s00775-025-02131-y","url":null,"abstract":"<div><p>Advances in bioelectronic and renewable energy technologies make it important for undergraduate students to learn about bioelectrochemistry, and courses in the chemical and biological sciences provide opportunities for them to do so. This review surveys the ways in which bioelectrochemistry appears in these degree programs and evaluates effective educational practices in each case. Three key pedagogical challenges are identified: bioelectrochemical concepts are often abstract, the terminology is confusing and variable, and relevant material is fragmented across the curriculum. The review makes five recommendations to address these challenges. Educators are advised to (1) signpost connections across the curriculum to promote topic integration, (2) provide explicit guidance on terminology to pre-empt confusion, (3) use vivid biological examples to capture student attention and interest, (4) use active learning techniques to strengthen conceptual links, and (5) adopt published laboratory exercises that allow students to put bioelectrochemical theory into practice. In each case, examples are given to support implementation and enhance undergraduate student appreciation of the field.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture><span>The alternative text for this image may have been generated using AI.</span></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 1-2","pages":"39 - 47"},"PeriodicalIF":2.7,"publicationDate":"2025-12-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-025-02131-y.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145814664","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Looking backward to move forward: a chemist’s perspective on the future of radiopharmaceuticals","authors":"Stacey E. Rudd","doi":"10.1007/s00775-025-02130-z","DOIUrl":"10.1007/s00775-025-02130-z","url":null,"abstract":"<div><p>Nuclear medicine has existed since the 1940s, but the clinical approval of a handful of new radiopharmaceutical agents in the last few years has thrust the field into the spotlight of modern cancer research. Now that radiopharmaceuticals have caught everyone’s attention, what are the future directions in this rapidly growing area? This commentary highlights some of the field’s successes and failures over the last few decades, explores emerging ideas for the next steps in radiopharmaceutical development, and ponders whether we are ready to revisit old ideas using a modern twist.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture><span>The alternative text for this image may have been generated using AI.</span></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 1-2","pages":"29 - 37"},"PeriodicalIF":2.7,"publicationDate":"2025-12-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145792908","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Olefin metathesis of phospholipids by Ruthenium-based catalysts in solution and on liposomes under biologically relevant conditions","authors":"Pina Eichert,&nbsp;Huriye Deniz Uzun,&nbsp;Sascha Heinrich,&nbsp;Thomas Günther Pomorski,&nbsp;Nils Metzler-Nolte","doi":"10.1007/s00775-025-02129-6","DOIUrl":"10.1007/s00775-025-02129-6","url":null,"abstract":"<div><p>The last decade has seen a lot of interest in classical organometallic catalysis performed intracellularly, or at least under biological conditions (37 °C, air, water). One such classical reaction is olefin metathesis (OM), which is extremely common in preparative organic chemistry, however under non-biological conditions (esp. organic solvents). For in vivo applications, both prokaryotic and eukaryotic applications would require the passage of the OM catalyst through the cell membrane, which already contains unsaturated olefins and thus potential substrates for OM. This work focuses on the question whether OM is catalysed in membranes containing unsaturated phospholipids. Initial experiments with the 2nd generation Hoveyda-Grubbs catalyst (<b>HGII</b>) showed self-metathesis of the membrane-forming phospholipids POPE, POPC, and POPG, while approximating biological conditions in solution (37 °C, air, neutral pH) with substrate conversions up to 58%. Subsequent experiments with DOPC in large unilamellar vesicles (LUVs) and in solution included a PEGylated (featuring increased water solubility) and a palmitoylated (with increased membrane mobility) <b>HGII</b> derivative. Both were successfully synthesised beforehand and comprehensively characterized. Membrane localisation of the catalysts was evaluated via size exclusion chromatography (SEC) followed by ICP-MS. Product analysis of OM was carried out after one hour and 24 h, respectively, via NMR, TLC, and LC-MS. The intra- and intermolecular OM products of DOPC were identified. First, substrate conversion was significantly diminished in the vesicles, however, the equilibrium state in vesicles was reached in much less time compared to solution (1 h in vesicles vs. 24 h in solution). To our surprise, a distinct difference in product selectivity between OM in solution and in vesicles was observed in that the intramolecular OM is much favoured in solution, while in LUVs, the main products are the result of intermolecular OM reactions. Our results prove that OM is readily catalysed in vesicles and indicate that the milieu of the lipid bilayer has a major impact on the product selectivity, reaction time and substrate conversion. While previous work has focused on the cytotoxicity of Hoveyda-Grubbs catalysts and their interaction with biomolecules, our present work provides valuable insights on what will happen when an OM catalyst like <b>HGII</b> is exposed to membranes in organisms. Moreover, using the results from this work, it may be possible to selectively modify membrane properties, and thereby cellular responsiveness to outside stress, by olefin metathesis in the future.</p></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 6-8","pages":"563 - 575"},"PeriodicalIF":2.7,"publicationDate":"2025-11-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-025-02129-6.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145601446","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Oxidative environments promote the formation of detergent-resistant IgG aggregates mediated by Cu(II) assessed by optical density: implications in vivo","authors":"Christian Saporito-Magriña,&nbsp;Lila Lopez-Montañana,&nbsp;María Laura Facio,&nbsp;Guadalupe Pagano,&nbsp;Aldana Rodriguez,&nbsp;Juan Ignacio Bellida,&nbsp;Marisa Gabriela Repetto","doi":"10.1007/s00775-025-02128-7","DOIUrl":"10.1007/s00775-025-02128-7","url":null,"abstract":"<div><p>Protein proclivity to aggregation leads to the formation of insoluble aggregates which slowly build up over the years within blood and different tissues. In humans, the content of these detergent resistant aggregates has been found increased in elder subjects compared to younger ones. The aggregation process is driven not solely by the presence of prone to aggregation proteins but by pro-aggregating agents such as Cu(II) which promotes the aggregation of IgG among others. Cu(II) and Zn(II) induce IgG reversible aggregates. However, co-incubation of Cu(II) with hydrogen peroxide (H₂O₂) renders the aggregate irreversibly insoluble upon metal removal which also becomes detergent resistant. Conversely, in the case of Zn(II)-induced aggregates, the addition of H₂O₂ in concentrations as high as 3 mM does not yield a detergent resistant aggregate. Contrarily to Cu(II), Zn(II) is redox inactive and unable to react with H₂O₂. Notably, the incubation of IgG with Cu(II) and low concentrations of H₂O₂ (50 µM) leads to the formation of soluble aggregates which can be detected by SDS-PAGE. Boiling allows partial dis-aggregation of the SDS-resistant aggregates and the migration pattern of boiled IgG oxidized in vitro by Cu(II)/H₂O₂ is similar to that observed in the aggregates from human sera. The presence of IgG was confirmed by western blot in SDS-resistant aggregates found in elder and young sera. Therefore, we speculate that Cu(II) reaction with H₂O₂ may contribute to IgG-enriched circulating protein aggregates and their clinical relevance should be further explored as they could resemble circulating immune-complexes which possess several pro-inflammatory features.</p></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 6-8","pages":"545 - 561"},"PeriodicalIF":2.7,"publicationDate":"2025-11-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145501316","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}