Biochimica et Biophysica Acta-Bioenergetics最新文献

{"title":"Energetics and evolution: Response to Martin","authors":"Michael Lynch","doi":"10.1016/j.bbabio.2025.149576","DOIUrl":"10.1016/j.bbabio.2025.149576","url":null,"abstract":"<div><div>A recent paper in this journal claims that prior estimates of the bioenergetic costs of producing cells are off by more than 100-fold. Here, it is shown that this conclusion is based on an erroneous interpretation of the methods previously employed by a diversity of authors and that the downstream arguments are conceptually flawed. Likewise, the author's claim that the establishment of the mitochondrion caused a quantum leap in bioenergetic capacity that spurred a revolution in eukaryotic innovation is inconsistent with empirical data and evolutionary theory.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149576"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145794981","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Substitution of Mg2+ cofactor with Ca2+ disrupts positive cooperativity in F1FO-ATP(hydrol)ase catalysis","authors":"Cristina Algieri ,&nbsp;Antonia Cugliari ,&nbsp;Fabiana Trombetti ,&nbsp;Salvatore Nesci","doi":"10.1016/j.bbabio.2025.149580","DOIUrl":"10.1016/j.bbabio.2025.149580","url":null,"abstract":"<div><div>The mitochondrial F₁F_O-ATPase is a dual-function enzyme that synthesizes ATP using the proton motive force and hydrolyzes ATP to reenergize the membrane.</div><div>Mg²⁺ is the physiological cofactor of F₁F_O-ATPase, enabling both ATP synthesis and hydrolysis, while Ca²⁺ supports only ATP hydrolysis.</div><div>Mg²⁺-dependent F₁F_O-ATPase exhibits positive cooperativity in ATP hydrolysis Hill coefficient (nHi) of 2.01 ± 0.21, whereas Ca²⁺-dependent activity shows Michaelian kinetics, nHi 1.41 ± 0.06.</div><div>Ca²⁺ acts as an uncompetitive inhibitor on Mg²⁺-dependent ATP hydrolysis, suggesting distinct binding sites and conformational effects.</div><div>The differential kinetic behavior underlies the enzyme's multifunctionality of F₁F_O-ATPase in physio-pathological conditions, depending on the cofactor.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149580"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145926423","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The contribution of D2-Arg265 to the molecular architecture of the quinone-Fe-bicarbonate acceptor complex of photosystem II","authors":"Victor Zhong ,&nbsp;Imre Vass ,&nbsp;Julian J. Eaton-Rye","doi":"10.1016/j.bbabio.2025.149578","DOIUrl":"10.1016/j.bbabio.2025.149578","url":null,"abstract":"<div><div>In Photosystem II (PS II) the D2 and D1 proteins provide binding sites for the primary (Q_A) and secondary (Q_B) plastoquinone electron acceptors, respectively. A non-heme iron is located between Q_A and Q_B that is coordinated by a bicarbonate ligand and two His residues from D1 (D1-His215 and D1-His272) and two His residues from D2 (D2-His214 and D2-His268). The symmetry of the quinone-Fe-acceptor complex extends to D1-Arg269, which has hydrogen bonds to D1-His272, and D2-Arg265 which has hydrogen bonds to D2-His268. We have examined the role of D2-Arg265 by creating the R265A and R265D mutants in the cyanobacterium <em>Synechocystis</em> sp. PCC 6803. Both mutants exhibited normal photoautotrophic growth, but showed a reduction in oxygen evolution in the presence of the PS II-specific electron acceptor 2,5-dimethyl-1,4-benzoquinone (DMBQ). Chlorophyll <em>a</em> fluorescence induction and decay kinetics were also inhibited in the presence of DMBQ and, in the presence of the native quinone, revealed slowed Q_A^{<strong>−</strong>} to Q_B electron transfer, together with impaired exchange between the Q_B-binding site and the plastoquinone pool. Addition of formate further inhibited electron transfer, consistent with weakened bicarbonate binding in the mutants, and thermoluminescence measurements revealed a decreased redox gap between Q_A and Q_B. Additionally, both mutants displayed heightened sensitivity to high light. These findings demonstrate that D2-Arg265 is important for stability of the acceptor side, bicarbonate-dependent electron transfer, and an optimal Q_B-binding site. All of our results are also consistent with the architecture of the quinone-Fe-bicarbonate complex supporting photoprotection and regulatory roles that are unique to oxygenic photosynthesis.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 2","pages":"Article 149578"},"PeriodicalIF":2.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145821800","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The internal alternative NADH dehydrogenase (Ndi1) is the electron input in the Saccharomyces cerevisiae respirasome","authors":"Italo Lorandi ,&nbsp;José Alfredo Hernández-Zúñiga ,&nbsp;Mercedes Esparza-Perusquía ,&nbsp;Genaro Matus-Ortega ,&nbsp;Héctor Vázquez-Meza ,&nbsp;Héctor Flores-Herrera ,&nbsp;Juan Pablo Pardo ,&nbsp;Federico Martínez ,&nbsp;Oscar Flores-Herrera","doi":"10.1016/j.bbabio.2025.149574","DOIUrl":"10.1016/j.bbabio.2025.149574","url":null,"abstract":"<div><div>Complex I is absent in mitochondria from <em>Saccharomyces cerevisiae</em>; instead, three rotenone-insensitive NADH dehydrogenases are present: two on the external (Nde1 and Nde2) and one on the internal (Ndi1) leaf of the inner mitochondrial membrane. In a previous work (1), we reported the presence of a supercomplex in <em>S. cerevisiae</em> constituted by the Ndi1 and complexes III₂ and IV with an apparent MW of 1600 kDa. In this work, respirasomes from WT and <em>NDE1Δ/NDE2Δ</em> strains were isolated, and their activities characterized. Kinetic characterization of NADH:DBQ oxidoreductase activity from respirasomes, as well as free Ndi1, showed V_max values of 0.85 ± 0.01, 0.82 ± 0.02, and 0.51 ± 0.02 μmol NADH oxidized·min⁻¹·mg⁻¹ for WT respirasome, <em>NDE1Δ/NDE2Δ</em> respirasome, and free Ndi1, respectively. The kinetic model for WT- and <em>NDE1Δ/NDE2Δ</em> respirasome was a Ping Pong Bi-Bi mechanism with two different stable enzyme forms, free (E) and modified enzyme (F); while the free Ndi1 exhibited a Random Bi-Bi mechanism with the ternary complex NADH-Ndi1-ubiquinone. This suggests that the interaction of Ndi1 with complexes III₂ and IV in the respirasome modifies its kinetic mechanism. Oxygen consumption values were 0.35 ± 0.07 and 0.34 ± 0.07 μmol O₂·min⁻¹·mg⁻¹ for WT and <em>NDE1Δ/NDE2Δ</em> respirasomes, respectively. The values for NADH/O₂ ratio were 2.4 ± 1.4 and 2.4 ± 1.6 for WT and <em>NDE1Δ/NDE2Δ</em> respirasomes, respectively, suggesting that electron flux from NADH to oxygen occurs in the <em>S. cerevisiae</em> respirasome. The electron transfer from NADH to oxygen was inhibited by flavone, antimycin A, or cyanide, but the NADH dehydrogenase activity of the respirasome was insensitive to antimycin A or cyanide, indicating that no codependence of respirasomal-Ndi1 activity occurs as reported in the <em>Ustilago maydis</em> respirasome. This result indicates that the activity of respirasomal Ndi1 may contribute to the quinol pool with no evidence of direct substrate channeling. This is the first evidence of the Ndi1 role as the electron input in the respirasome from <em>S. cerevisiae</em>.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 1","pages":"Article 149574"},"PeriodicalIF":2.7,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145589806","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Increase in spillover and excitation energy dissipation during wet–dry transitions in the desert green alga Chlorella ohadii","authors":"Soma Kawamura ,&nbsp;Makio Yokono ,&nbsp;Chiyo Noda ,&nbsp;Jun Minagawa","doi":"10.1016/j.bbabio.2025.149573","DOIUrl":"10.1016/j.bbabio.2025.149573","url":null,"abstract":"<div><div><ul><li><span>•</span><span><div>Under drought, lack of an electron source (water) reduces the capacity of oxygen-evolving photosynthesis.</div></span></li><li><span>•</span><span><div>Consequently, even under low light, excess excitation energy may be generated, which is harmful as it leads to generation of reactive oxygen species.</div></span></li><li><span>•</span><span><div>When the desert green alga <em>Chlorella ohadii</em> undergoes desiccation, first photosystem II binds to photosystem I via LHCII to establish energy transfer pathways, and then excitation energy dissipation induced by a quencher is initiated.</div></span></li><li><span>•</span><span><div>This strategy may provide efficient protection of the entire photosynthetic apparatus during early stages of desiccation, when the available quencher may be insufficient.</div></span></li></ul></div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 1","pages":"Article 149573"},"PeriodicalIF":2.7,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145092999","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mechanism of Na+ ions contribution to the generation and maintenance of a high inner membrane potential in mitochondria","authors":"Victor V. Lemeshko","doi":"10.1016/j.bbabio.2025.149571","DOIUrl":"10.1016/j.bbabio.2025.149571","url":null,"abstract":"<div><div>A recent revision of the chemiosmotic theory was reported by Hernansanz-Agustín and coauthors as a discovery that a Na⁺ gradient across the mitochondrial inner membrane equates with the H⁺ gradient and contributes up to half of the inner membrane potential, without an explanation of the possible underlying mechanism. Based on the experimental data of these and other authors, and performed biophysical estimations, I propose a mechanism by which both the reported fast-acting Na⁺/H⁺ exchanger, associated with the complex I of the respiratory chain, and Na⁺ electrodiffusion in the intracristae space and the matrix allow maintenance of a high membrane potential.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1867 1","pages":"Article 149571"},"PeriodicalIF":2.7,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145007521","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Vibrational cooling of monomeric bacteriochlorophylls in reaction centers of purple bacteria studied by time-resolved fluorescence spectroscopy","authors":"Andrei G. Yakovlev ,&nbsp;Alexandra S. Taisova","doi":"10.1016/j.bbabio.2025.149570","DOIUrl":"10.1016/j.bbabio.2025.149570","url":null,"abstract":"<div><div>Photosynthesis in bacteria, algae, and plants begins with the absorption of light energy by (bacterio)chlorophyll molecules, part of which is then converted into heat, leading to a transient change in molecular temperature. We investigated this phenomenon in reaction centers (RCs) of the purple bacterium <em>Rhodobacter</em> (<em>Rba</em>.) <em>sphaeroides</em> using picosecond fluorescence spectroscopy. Exclusion of charge separation processes using the VR(L157) mutation allowed us to record the spectral dynamics of fluorescence of monomeric BChl <em>a</em> molecules. We found that excitation of RCs into the Soret band results in significant heating of BChl <em>a</em> by ~160 K with subsequent vibrational cooling, which manifests itself in a dynamic narrowing of the BChl <em>a</em> fluorescence spectrum with two characteristic times of 5 and 16 ps. The weaker heating by ~65 K and cooling with a characteristic time of 7.5 ps are observed upon excitation of RCs into the Q_x band. Excitation into the Q_у band does not result in any noticeable heating of BChl <em>a</em>. Difference absorption spectroscopy of tryptophan in the 280 nm region showed that the observed dynamics of the BChl <em>a</em> fluorescence spectrum are not associated with the dielectric rearrangement of the RCs protein matrix. Analysis of the obtained data using the phenomenological model of vibrational cooling led to the conclusion that during heat diffusion from excited BChl <em>a</em>, several amino acid residues from the immediate environment of BChl <em>a</em> act as the first solvation shell (FSS). At the first, faster stage, heat is transferred from BChl <em>a</em> to FSS, and at the second stage, FSS transfers heat to the protein matrix of RCs. Our work has shown the importance of taking into account vibrational cooling when studying the primary processes of photosynthesis.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 4","pages":"Article 149570"},"PeriodicalIF":2.7,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144904589","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dynamic binding of acetogenin-type inhibitors to mitochondrial complex I revealed by photoaffinity labeling","authors":"Misaki Nishida ,&nbsp;Cristina Pecorilla ,&nbsp;Takahiro Masuya ,&nbsp;Keitaro Hirano ,&nbsp;Masato Abe ,&nbsp;Oleksii Zdorevskyi ,&nbsp;Vivek Sharma ,&nbsp;Hideto Miyoshi ,&nbsp;Masatoshi Murai","doi":"10.1016/j.bbabio.2025.149566","DOIUrl":"10.1016/j.bbabio.2025.149566","url":null,"abstract":"<div><div>Acetogenins isolated from the <em>Annonaceae</em> plant family are potent inhibitors of mitochondrial NADH-ubiquinone (UQ) oxidoreductase (complex I). Since acetogenins have a markedly different chemical framework from other complex I inhibitors, studying their inhibitory action offers valuable insights into the mechanism of complex I inhibition. A cryo-EM structure of mouse complex I with a bound ~35 Å-long acetogenin derivative suggested that acetogenins bind along the full length of the predicted UQ-accessing tunnel, with their γ-lactone ring orientating toward the iron‑sulfur cluster N2. However, this binding mode does not fully explain the structure–activity relationships of various acetogenin derivatives. To further elucidate their inhibition mechanism, we conducted photoaffinity labeling experiments in bovine heart SMPs using a photoreactive acetogenin derivative DLA-1, containing a small photolabile diazirine near the γ-lactone ring. DLA-1 labeled both the complex I subunits 49-kDa and ND1, which define the architecture of “top” and “bottom” regions of the canonical UQ-accessing tunnel, respectively. Proteomic analysis revealed that the labeled sites in ND1 are not within the tunnel's interior, whereas in the case of 49-kDa subunit, part of the tunnel's inner region is labeled. To investigate the molecular basis of acetogenin binding, we performed atomistic molecular dynamics simulations of DLA-1 and a natural-type acetogenin analog in the UQ-accessing tunnel. The simulation data indicate that DLA-1 is relatively rigid yet adopts multiple conformations and interacts with several regions in the tunnel including the residues identified by photoaffinity labeling. Based on these results, we discuss the binding modes of acetogenin analogs to complex I.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 4","pages":"Article 149566"},"PeriodicalIF":3.4,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144545921","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Photodamage and excitation energy quenching in PSII: A time-resolved fluorescence study in Arabidopsis","authors":"Cleo Bagchus ,&nbsp;Herbert van Amerongen ,&nbsp;Emilie Wientjes","doi":"10.1016/j.bbabio.2025.149569","DOIUrl":"10.1016/j.bbabio.2025.149569","url":null,"abstract":"<div><div>Photosynthesis is driven by light absorbed in photosystem (PS) I and II. Paradoxically, light can also inactivate photosynthesis, mainly by damage to PSII. The light-dependent decrease in functional PSII, referred to as photoinhibition, is initially accompanied by an increase of excitation quenching, energy dissipation characterized by a decline in the lifetime and yield of chlorophyll fluorescence. In plants, research has not yet been performed on the effect of photoinhibition on the fluorescence lifetime of PSII in conditions where the PSII reaction centers are closed or remain open (capable of performing photochemistry).</div><div>In this work, we studied the effect of photoinhibition on the fluorescence lifetime of PSII in <em>Arabidopsis thaliana</em> using time-resolved fluorescence measurements with a streak-camera setup in both closing (F_m) and non-closing (F_o) conditions. Measurements under F_m conditions in the <em>chlorina</em> mutant, lacking peripheral antenna, demonstrate formation of a photoinhibitory quencher in the PSII core complex. In F_o_, the average fluorescence lifetime of PSII increases upon induction of photoinhibition. This could be due to the degradation of quenched PSII core reaction center protein by FtsH proteases, which leads to unquenched and dysfunctional PSII. We tested this hypothesis by comparing WT plants with the FtsH2 lacking mutant. Based on the similar behavior, we conclude that degradation by FtsH proteases is not the main cause of the increase. Instead this increase is caused by the larger antenna size of still functional PSII. These findings provide new insights into the impact of photoinhibition on the PSII fluorescence lifetime in <em>A. thaliana</em>.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 4","pages":"Article 149569"},"PeriodicalIF":2.7,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144849506","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Human VDAC3 as a sensor of the intracellular redox state: contribution to cytoprotection mechanisms in oxidative stress","authors":"Martyna Baranek-Grabińska ,&nbsp;Tomasz Skrzypczak ,&nbsp;Hanna Kmita ,&nbsp;Andonis Karachitos","doi":"10.1016/j.bbabio.2025.149565","DOIUrl":"10.1016/j.bbabio.2025.149565","url":null,"abstract":"<div><div>Voltage-dependent anion channels (VDACs) are essential for mitochondrial function, facilitating the exchange of metabolites between the cytosol and mitochondria. This study investigated the role of human VDAC paralogs, hVDAC1, hVDAC2, and hVDAC3, in maintaining mitochondrial function under oxidative stress in <em>Saccharomyces cerevisiae</em> strains lacking endogenous VDACs (encoded by <em>POR1</em> and <em>POR2</em>) and antioxidant enzymes, i.e., superoxide dismutases (encoded by <em>SOD1</em> and <em>SOD2</em>). The yeast cells expressing hVDAC3 showed stable growth under oxidative stress, maintained mitochondrial membrane potential and morphology, exhibited reduced superoxide anion levels, and achieved efficient ATP synthesis with minimal proton leak. In contrast, the cells expressing hVDAC1 or hVDAC2 presented impaired mitochondrial function which was supported by differences in bioenergetic profiles including ATP synthesis and proton leak but also FCCP uncoupling capacity and spare respiratory capacity. The cysteine-depleted variant of hVDAC3 (hVDAC3ΔCys) showed impaired cell growth under stress conditions, indicating that the cysteine residues in hVDAC3 are essential for its protective role. These findings highlight the unique protective function of hVDAC3 under oxidative stress, which is attributed to efficient metabolite transport and regulation via cysteine oxidation.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 4","pages":"Article 149565"},"PeriodicalIF":3.4,"publicationDate":"2025-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144517673","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}