Journal of Biological Inorganic Chemistry最新文献

{"title":"Detection of a clamp-shaped conformation of a neuronal nitric oxide synthase construct by pulsed EPR.","authors":"Andrei V Astashkin, Yadav Prasad Gyawali, Ting Jiang, Huayu Zheng, Changjian Feng","doi":"10.1007/s00775-025-02126-9","DOIUrl":"https://doi.org/10.1007/s00775-025-02126-9","url":null,"abstract":"<p><p>Nitric oxide synthase (NOS) is an enzyme responsible for the production of nitric oxide in living organisms. Structurally, it is a homodimer composed of multiple domains connected by random coil tethers. The resulting structural flexibility, along with the diverse conformational states it enables, is essential for NOS function and remains an active area of investigations. Here, we studied the docking interactions between the reductase domains of NOS subunits. To probe these interactions, a nitroxide-based bifunctional spin label was attached to each T34C/S38C calmodulin (CaM) molecule bound to the CaM-binding region of the tether, which connects the oxygenase and flavin mononucleotide (FMN) domains in each subunit of the homodimeric oxygenase/FMN (oxyFMN) construct of rat neuronal NOS (nNOS). The magnetic dipole interaction between the spin labels was detected by 2 + 1 electron spin echo (ESE) methods. The experimental 2 + 1 ESE traces were interpreted using the Monte Carlo calculations of NOS conformational distributions. The results unequivocally show that at the estimated effective temperature of the frozen conformational distribution, T_ef ≈ 200 K, a large proportion of the oxyFMN proteins (~ 55%) adopt a clamp-shaped conformation in which the FMN domains of different NOS subunits dock with each other. The stabilization energy of this docking complex (i.e., docking energy) was estimated in the model of isotropic interaction as - 7.2kT_ef ≈ - 2.9 kcal/mol. The identification of this clamp-shaped conformation suggests it as an intermediate structural state that may influence NOS catalytic efficiency by facilitating the FMN-heme interdomain electron transfer through constraining the conformational space accessible to the FMN domain as it approaches its docking positions at the heme domain.</p>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145068817","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":"Interactions of elongated dinuclear metallo-cylinders with DNA three-way and four-way junctions.","authors":"Samuel J Dettmer, Hannah M P Stock, Michael J Hannon","doi":"10.1007/s00775-025-02123-y","DOIUrl":"https://doi.org/10.1007/s00775-025-02123-y","url":null,"abstract":"<p><p>Non-canonical DNA structures play important roles in processing of the genetic code. Three-way (3WJ) and four-way (4WJ) junctions are dynamic, multi-stranded structures containing an open cavity at the centre. We have previously demonstrated that supramolecular dinuclear metallo-cylinders bind well inside 3WJ cavities, having an optimally complementary size and shape match, cationic charge to bind the DNA anion, as well as the ability to π‑stack with the branchpoint nucleobases. Herein, we show that a longer metallo-cylinder with a similar but extended central π surface binds to both 3WJ and 4WJ structures with good selectivity over double-stranded DNA. Experimental investigations, informed by molecular dynamics (MD) simulations, reveal that whilst this longer cylinder can bind 3WJs as the previously studied cylinders, the extended π surface of the cylinder now also facilitates 4WJ binding. The simulations capture two metastable 4WJ conformations -one resembling a 3WJ, and another where the extended length enables the cylinder to angle into and stabilise a rhombus-shaped 4WJ cavity. The ability to tune the structure of supramolecular assemblies is important for targeting different DNA structures with varying specificity, and in this work, we demonstrate the usefulness of overall length as a parameter for modulating DNA binding.</p>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145063090","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 tris(pyrazolyl)-based model for the aminocyclopropane carboxylic acid oxidase and its behavior towards oxidants.","authors":"Lars Müller, Charikleia Tzatza, Santina Hoof, A Jalila Simaan, Christian Limberg","doi":"10.1007/s00775-025-02125-w","DOIUrl":"https://doi.org/10.1007/s00775-025-02125-w","url":null,"abstract":"<p><p>A low-molecular-weight analog of the 1-aminocyclopropane carboxylic acid oxidase (ACCO), [Tp^MesFeACC], 1, where the (His₂Asp)iron(II) moiety is mimicked by a hydrotris(3-mesitylpyrazol-1-yl)borato iron(II) unit, to which the natural substrate aminocyclopropane carboxylate is coordinated, has been accessed and structurally characterized. It was found to react slowly with O₂ to yield the biological product ethylene. To create models of the intermediates proposed as part of the catalytic cycle of the ACCO 1 was treated with tBuOOH and mCPBA at low temperatures, which generated the respective Fe^IIIOOtBu and Fe^IV=O intermediates as shown by spectroscopic analysis. Studies on their behavior upon annealing reveal a non-biomimetic reactivity.</p>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145051554","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":"The important interplay between metal ions and the intermediate filament protein vimentin.","authors":"Estely J Carranza, Dylan T Murray, Marie C Heffern","doi":"10.1007/s00775-025-02124-x","DOIUrl":"https://doi.org/10.1007/s00775-025-02124-x","url":null,"abstract":"<p><p>Vimentin is a principal intermediate filament (IF) protein that is essential for maintaining cytoskeleton architecture and cellular mechanical integrity. Growing evidence is revealing that metal ions play critical roles in modulating the structure, assembly, and mechanics of vimentin IFs. Despite this, a detailed molecular-level understanding of vimentin-metal interactions and its functional consequences remains incomplete. This review summarizes the current knowledge of metal-induced effects on the structural and mechanical properties of vimentin and highlights how post-translational modifications and cytoskeletal dynamics may alter these metal-protein interactions. Advancing our understanding of the interplay between metal ions and vimentin IFs will enhance our comprehension of the complex mechanisms governing the versatile functions of vimentin and other IF proteins in health and disease.</p>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145005798","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":"Novel phenanthroline-based ruthenium complex as a promising antimicrobial agent.","authors":"Pedro L N Teixeira, Ana C S Gondim, Tercio F Paulo, Eduardo H S Sousa, Luiz G F Lopes, Alejandro P Ayala, Ellen A Malveira, Edson H Teixeira, Mayron A Vasconcelos, Alda K M Holanda","doi":"10.1007/s00775-025-02122-z","DOIUrl":"https://doi.org/10.1007/s00775-025-02122-z","url":null,"abstract":"<p><p>A novel ruthenium(II) compound, cis-[Ru(phen)₂(4-bzpy)(Cl)](PF₆) (complex I), where phen = 1,10-phenanthroline and 4-bzpy = 4-benzoylpyridine, was synthesized and fully characterized using electrochemical and spectroscopic methods, and its structure was determined by single-crystal X-ray diffraction. Density functional theory (DFT) and time-dependent DFT calculations were performed to shed light on the electronic structure and nature of the vibrational and electronic transitions. The photochemical behavior of complex I in aqueous solution showed that irradiation with blue light (453 nm) promoted the release of the coordinated 4-bzpy ligand originating cis-[Ru(phen)₂(H₂O)(Cl)]⁺ ion, as identified by NMR and electronic spectroscopy. Moreover, complex I exhibited a great ability to cleave DNA molecules upon blue light irradiation, which was associated with the production of reactive oxygen species (singlet oxygen and superoxide anion). In this study, we also investigated the antimicrobial activity of complex I along with a similar compound, cis-[Ru(bpy)₂(4-bzpy)(Cl)](PF₆) (complex II), their precursors [Ru(bpy)₂Cl₂] and [Ru(phen)₂Cl₂], and the free ligand 4-bzpy. These two ruthenium complexes I and II have a common auxiliary ligand 4-bzpy, but distinct chelating ligands (phenanthroline or 2,2'-bipyridine, bpy). Notably, both complexes showed promising antibacterial activity against Gram-positive bacterial strains of Staphylococcus aureus and Staphylococcus epidermidis. However, complex I showed a superior antibacterial effect compared with complex II, supporting the important role of the phen ligand, likely providing greater lipophilicity to this compound.</p>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144938201","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":"Biogenic silver nanoparticles from chamomile incorporated in hydrogels for high transparent non-infectiveness contact lenses.","authors":"Panagiotis K Raptis, Christina N Banti, Christina Papachristodoulou, Sotiris K Hadjikakou","doi":"10.1007/s00775-025-02121-0","DOIUrl":"https://doi.org/10.1007/s00775-025-02121-0","url":null,"abstract":"<p><p>Chamomile extract (CHA) was employed in the synthesis of silver nanoparticles (AgNPs(CHA)). These nanoparticles were incorporated into a hydroxyethyl methacrylate (pHEMA) matrix during polymerization at concentrations of 1 mg/mL (pHEMA@AgNPs(CHA)_1) and 2 mg/mL (pHEMA@AgNPs(CHA)_2). The resulting materials- AgNPs(CHA), pHEMA@AgNPs(CHA)_1, and pHEMA@AgNPs(CHA)_2 -were characterized using a plethora of analytical techniques, including Refractive Index (RI), X-ray fluorescence (XRF) spectroscopy, X-ray powder diffraction (XRPD), thermogravimetric-differential thermal analysis (TG-DTA), differential scanning calorimetry (DSC), ultraviolet-visible (UV-Vis) spectroscopy, and attenuated total reflection Fourier-transform infrared (ATR-FTIR) spectroscopy in the solid state, as well as UV-Vis spectroscopy in solution. XRPD analysis revealed a crystallite size of 8.02 nm, while the diameter of the nanoparticles, estimated using the λmax of the Surface Plasmon Resonance (SPR) spectrum, was 37 nm. The antimicrobial properties of the materials were evaluated against Gram-negative bacteria, Pseudomonas aeruginosa and Escherichia coli, as well as Gram-positive bacteria, Staphylococcus epidermidis and Staphylococcus aureus. These pathogens are commonly implicated in microbial keratitis. Antimicrobial efficacy was assessed using Minimum Inhibitory Concentration (MIC), Minimum Bactericidal Concentration (MBC), and Inhibitory Zones (IZs). The IZs for P. aeruginosa, E. coli, S. epidermidis, and S. aureus following incubation with paper discs soaked in 1 mg/mL of AgNPs(CHA) were 16.0 ± 0.6 mm, 11.1 ± 0.9 mm, 15.8 ± 1.2 mm, and 15.1 ± 0.2 mm, respectively. Bacterial viability after incubation with hydrogel discs of pHEMA@AgNPs(CHA)_1 showed reductions to 0.9 ± 0.2%, 100.0 ± 0.0%, 1.9 ± 1.0%, and 4.4 ± 1.5% for P. aeruginosa, E. coli, S. epidermidis, and S. aureus, respectively. Additionally, no toxic effects were observed on human corneal epithelial cells (HCECs). These findings suggest that pHEMA@AgNPs(CHA)_1 has potential as a promising candidate for developing non-infectious contact lenses.</p>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":" ","pages":""},"PeriodicalIF":2.7,"publicationDate":"2025-08-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144783166","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":"Magnetic interactions between metal sites in complex enzymes","authors":"Biplab K. Maiti,&nbsp;Isabel Moura,&nbsp;José J. G. Moura","doi":"10.1007/s00775-025-02120-1","DOIUrl":"10.1007/s00775-025-02120-1","url":null,"abstract":"<div><p>Magnetic interactions between iron–sulfur (Fe/S) clusters and transition metal centers such as nickel, molybdenum, and copper play a central role in the function of key metalloenzymes. These interactions, which arise from electronic coupling, spin exchange, and spatial arrangement, directly influence redox behavior and catalytic efficiency. This review highlights three distinct complex enzymes—[NiFe] hydrogenases, mononuclear molybdenum-containing xanthine oxidase (XO) family, and [NiFe] and [MoCu] carbon monoxide dehydrogenases (CODHs)—as paradigms for understanding (Fe/S)-metal center interactions. In [NiFe] hydrogenases, (Fe/S) clusters serve as electron relays that magnetically interact with the catalytic [NiFe] active site. In XO-type enzymes, a mononuclear Mo center is functionally and magnetically coupled to nearby Fe/S clusters, modulating substrate reduction and electron transfer. Similarly, in CODHs, both [NiFe]—and [MoCu]-dependent variants exhibit strong magnetic communication between metal active sites and surrounding Fe/S clusters, crucial for CO₂/CO interconversion. Advanced spectroscopic approaches, particularly electron paramagnetic resonance (EPR) and related techniques, combined with theoretical modelling, have provided deep insights into the electronic structures and dynamic interactions within these metalloenzymes. Understanding these magnetic interactions not only sheds light on fundamental electron-transfer and enzymatic mechanisms but also guides the design of bioinspired catalysts and energy-conversion technologies. </p><h3>Graphical abstract</h3>\u0000<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 4-5","pages":"329 - 344"},"PeriodicalIF":2.7,"publicationDate":"2025-07-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12316806/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144697337","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":"Disulfide-based 2-pyridyl-hydrazone prochelators induce iron deprivation and oxidative stress in ovarian cancer cells","authors":"Jacob B. Fussell,&nbsp;Jake P. Shaw,&nbsp;Madison A. Grams,&nbsp;Yu-Shien Sung,&nbsp;Ren-Hua Jheng,&nbsp;Andrei V. Astashkin,&nbsp;Elisa Tomat","doi":"10.1007/s00775-025-02119-8","DOIUrl":"10.1007/s00775-025-02119-8","url":null,"abstract":"<div><p>Alterations of iron homeostasis are characteristic of malignant behavior and have been associated with poor prognosis in ovarian cancer patients. Iron-binding chelators are currently under investigation as potential cancer therapeutics because they allow manipulation of iron availability and redox chemistry. In addition, the design of prochelator systems enables the release of iron-binding chelators upon cell entry and therefore the sequestration of intracellular (rather than systemic) iron. We report the synthesis and biological evaluation of disulfide-based prochelators featuring a 2-pyridyl-hydrazone motif and resulting in a tridentate (<i>S,N,N</i>) donor set as found in several antiproliferative chelators (e.g., Triapine, Dp44mT, DpC, COTI-2). Upon disulfide reduction and iron(II) coordination, the chelators stabilize ferric complexes that are redox-active in neutral aqueous conditions. Symmetric prochelator (PH3-S)₂ and glucose conjugate G6PH3 have antiproliferative, pro-apoptotic effects in A2780 ovarian carcinoma cells. Both compounds sequester intracellular iron and impact the expression of the transferrin receptor TfR1 and the iron storage protein ferritin. Oxidative stress is found to be a component of the mechanism of action of these prochelators. Accordingly, the preformed iron complex FePH3 also leads to apoptosis and iron dysregulation, and its toxicity is enhanced when the antioxidant capacity of the cells is impaired. The incorporation of the 2-pyridyl-hydrazone motif in disulfide-based prochelators therefore combines iron sequestration with pro-oxidant effects that could enhance the pharmacological profile of this chelation approach for cancer applications.</p><h3>Graphical Abstract</h3>\u0000<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 4-5","pages":"443 - 452"},"PeriodicalIF":2.7,"publicationDate":"2025-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144537688","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":"Au(I)-based compounds inhibit nsp14/nsp10 and nsp13 (helicase) to exert anti-SARS-CoV-2 properties","authors":"Jingxin Chen,&nbsp;Xueying Wei,&nbsp;Chun-Lung Chan,&nbsp;Kaiming Tang,&nbsp;Shuofeng Yuan,&nbsp;Hongyan Li,&nbsp;Hongzhe Sun","doi":"10.1007/s00775-025-02118-9","DOIUrl":"10.1007/s00775-025-02118-9","url":null,"abstract":"<div><p>Au(I) compounds have long been associated with medicine for the treatment of various diseases, especially auranofin has been used for the treatment of rheumatoid arthritis. In addition, Au(I) based compounds also exhibit anti-cancer, anti-bacteria properties. The recent prevalence of the COVID-19 pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has aroused attention to investigate the antiviral potential of Au(I) compounds. Herein we demonstrate the pan-anti-SARS-CoV-2 activity of Au(I) metallodrugs in mammalian cells. We synthesized a panel of Au(I)-based compounds and found that these compounds could effectively inhibit the exoribonuclease and methyltransferase activities of SARS-CoV-2 nsp14/nsp10 complex, and the ATPase and DNA unwinding activities of SARS-CoV-2 nsp13 (helicase). Mechanistic studies reveal that Au(I) can not only displace the critical Zn(II) ions from nsp14/nsp10 complex and nsp13 but also changes the secondary and quaternary structure of nsp14 and perturbate the DNA unwinding of nsp13 by disrupting the ATP binding. This study illustrates a multi-target feature Au(I) compounds/drug agents for the viruses, highlighting their potential as pan-anti-SARS-CoV-2 (or relevant viruses) agents.</p><h3>Graphical Abstract</h3>\u0000<div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 4-5","pages":"425 - 441"},"PeriodicalIF":2.7,"publicationDate":"2025-06-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12316777/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144324105","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":"Bioinorganic chemistry: where from and where to?","authors":"Clotilde Policar","doi":"10.1007/s00775-025-02112-1","DOIUrl":"10.1007/s00775-025-02112-1","url":null,"abstract":"<div><p>Bioinorganic chemistry is a multidisciplinary field that bridges the apparent divide between inorganic chemistry and biology. The very name “bioinorganic” is an intriguing oxymoron, as “inorganic” chemistry traditionally refers to the study of the inanimate world, while the “bio” prefix refers to living systems. Bioinorganic chemistry focuses on metallic systems within biological environments, with the dual aims of better understanding these natural systems and leveraging the solutions developed through evolution to design new industrial or therapeutic applications. As a close cousin of the field of metallomics, bioinorganic chemistry shares the fundamental principles that underpin metallomics’ systemic analyses of metal-containing biomolecules. In this article, we trace the historical development of bioinorganic chemistry, highlighting its recent advancements and outlining future research challenges in this dynamic interdisciplinary area.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"30 4-5","pages":"313 - 328"},"PeriodicalIF":2.7,"publicationDate":"2025-06-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144245579","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}