Biochimica et Biophysica Acta-Bioenergetics最新文献

{"title":"Structural integrity and near-infrared absorption of the LH1 complex of Thermochromatium tepidum: Influence from the C-terminal lysine residues of LH1 α-polypeptide","authors":"Yi-Hao Yan ,&nbsp;Yu-Qian Li ,&nbsp;Mei-Juan Zou ,&nbsp;Long-Jiang Yu ,&nbsp;Jian-Ping Zhang","doi":"10.1016/j.bbabio.2025.149545","DOIUrl":"10.1016/j.bbabio.2025.149545","url":null,"abstract":"<div><div>The light-harvesting complex 1-reaction center (LH1-RC) photosystem of the thermophilic purple sulfur bacterium <em>Thermochromatium</em> (<em>Tch</em>.) <em>tepidum</em> exhibits a near-infrared LH1-Q_y absorption band at 915 nm as regulated by binding calcium ions (Ca²⁺). To further explore the possible involvement of the C-terminal lysine residues of the LH1 α-polypeptide, we have genetically engineered a <em>Rhodospirillum rubrum</em> mutant strain to yield the site-directed modifications of the terminal α-Lys60 and α-Lys61 residues of <em>Tch</em>. <em>tepidum</em> LH1 α-polypeptide. Four of the LH1 mutants exhibit a subtle blue shift of 3 nm upon deletion or substitution of the lysine residues, however, they display over 40 nm blue shifts upon Ca²⁺ removal by ethylene diamine tetraacetic acid (EDTA) treatment. Spectral properties of native <em>Tch</em>. <em>tepidum</em> LH1-RC, the LH1-only, and the mutant LH1-only complexes are compared on a structural basis, which allows us to conclude that the C-terminal lysine residues and the Ca²⁺ binding <em>synergistically</em> affect the structural integrity and the LH1-Q_y spectral shift. This work demonstrates a methodology for the genetic manipulation of photosynthetic proteins lacking mutagenesis information, and may shed light on understanding the detailed structural factors involved in tuning the LH1-Q_y absorption.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149545"},"PeriodicalIF":3.4,"publicationDate":"2025-02-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143378758","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":"Atypical absorption response to the trans-thylakoid electric field in the acidothermophilic red algae Cyanidioschyzon merolae and Galdieria partita","authors":"Guan-Lin Wu ,&nbsp;Shin-Ying Tzeng ,&nbsp;Benjamin Bailleul ,&nbsp;Julien Sellés ,&nbsp;You-Yuan Zhang ,&nbsp;Han-Yi Fu","doi":"10.1016/j.bbabio.2025.149544","DOIUrl":"10.1016/j.bbabio.2025.149544","url":null,"abstract":"<div><div>An absorption change responding to the change in the trans-thylakoid electric field (Δψ), also known as the electrochromic shift (ECS) signal, is widely used to probe multiple photosynthetic processes. The ECS signals either display a linear response of absorption changes to Δψ, independent of the trans-thylakoid electric field preexisting before actinic light (ψ_O), or a quadratic response, dependent on ψ_O. In the acidothermophilic red algae <em>Cyanidioschyzon merolae</em> and <em>Galdieria partita</em>, the absorption changes induced by single turnover saturating light flashes were affected by external pH. The effects of elevated external pH on the flash-induced absorption changes were explained by diminished ψ_O, as shown with the treatment of ionophores. We identified three contributions to the absorption changes: c-type cytochrome oxidized-minus-reduced signal and ECS signals showing both ψ_O-dependent and ψ_O-independent responses. Based on this, we could reveal that the effects of elevated external pH on the flash-induced absorption changes were due to variations of ψ_O, which in turn changed the contribution of the ψ_O-dependent ECS, as shown with the treatment of ionophores. Further analysis revealed that the ψ_O-dependent ECS signal exhibited a quadratic response to Δψ at low ψ_O, but the quadraticity was lost at higher ψ_O, providing insights for comprehending the atypical nature of the ECS signal. Our approach to identifying the ψ_O-dependent and ψ_O-independent ECS signals enables the ECS-based measurements for further investigation of the bioenergetics of electron and proton transport in red algae.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149544"},"PeriodicalIF":3.4,"publicationDate":"2025-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143383713","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":"Circadian clockwork controls the balance between mitochondrial turnover and dynamics: What is life … without time marking?","authors":"Olga Cela ,&nbsp;Rosella Scrima ,&nbsp;Michela Rosiello ,&nbsp;Consiglia Pacelli ,&nbsp;Claudia Piccoli ,&nbsp;Mirko Tamma ,&nbsp;Francesca Agriesti ,&nbsp;Gianluigi Mazzoccoli ,&nbsp;Nazzareno Capitanio","doi":"10.1016/j.bbabio.2025.149542","DOIUrl":"10.1016/j.bbabio.2025.149542","url":null,"abstract":"<div><div>Circadian rhythms driven by biological clocks regulate physiological processes in all living organisms by anticipating daily geophysical changes, thus enhancing environmental adaptation. Time-resolved serial multi-omic analyses in vivo, ex vivo, and in synchronized cell cultures have revealed rhythmic changes in the transcriptome, proteome, and metabolome, involving up to 50 % of the mammalian genome. Mitochondrial oxidative metabolism is central to cellular bioenergetics, and many nuclear genes encoding mitochondrial proteins exhibit both circadian and ultradian oscillatory expression. However, studies on mitochondrial DNA (mtDNA) gene expression remain incomplete. Using a well-established in vitro synchronization protocol, we investigated the time-resolved expression of mtDNA genes coding for respiratory chain complex subunits, revealing a rhythmic profile dependent on BMAL1, the master circadian clock transcription factor. Additionally, the expression of genes coding for key mitochondrial biogenesis transcription factors, PGC1a, NRF1, and TFAM, showed BMAL1-dependent circadian oscillations. Notably, LC3-II, involved in mitophagy, displayed a similar in-phase circadian expression, thereby maintaining stable respiratory chain complex levels. Moreover, we found that simultaneous mitochondrial biogenesis and degradation occur in a coordinated manner with cycles in organelle dynamics, leading to rhythmic changes in mitochondrial fission and fusion. This study provides new insights into circadian clock regulation of mitochondrial turnover, emphasizing the importance of temporal regulation in cellular metabolism. Understanding these mechanisms opens potential therapeutic avenues for targeting mitochondrial dysfunctions and related metabolic disorders.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149542"},"PeriodicalIF":3.4,"publicationDate":"2025-01-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143069253","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":"Commentary: Why do many cell biology papers contain fundamental bioenergetic errors?","authors":"David G. Nicholls","doi":"10.1016/j.bbabio.2025.149541","DOIUrl":"10.1016/j.bbabio.2025.149541","url":null,"abstract":"<div><div>To professional bioenergeticists, the thermodynamic and kinetic constraints on mitochondrial function are self-evident. It is therefore profoundly concerning that high-profile cell biology papers continue to appear containing fundamental bioenergetic errors that appear to have evaded the scrutiny of the principal investigator, co-authors, editors and, apparently, at least some of the referees. The problem is not new, and seems to stem from a perception that bioenergetics is a ‘difficult’ subject, both at undergraduate level, if it is taught in any depth, and in research, where cell biologists are faced with biophysical concepts such as protonmotive force, ion flux, redox potential and Gibbs free energy.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149541"},"PeriodicalIF":3.4,"publicationDate":"2025-01-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143015597","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":"Clinical ischemia-reperfusion injury: Driven by reductive rather than oxidative stress? A narrative review","authors":"Michèle J.C. de Kok ,&nbsp;Alexander F.M. Schaapherder ,&nbsp;Jonna R. Bloeme - ter Horst ,&nbsp;Maria Letizia Lo Faro ,&nbsp;Dorottya K. de Vries ,&nbsp;Rutger J. Ploeg ,&nbsp;Jaap A. Bakker ,&nbsp;Jan H.N. Lindeman","doi":"10.1016/j.bbabio.2025.149539","DOIUrl":"10.1016/j.bbabio.2025.149539","url":null,"abstract":"<div><div>Ischemia-reperfusion (IR) injury remains a major contributor to organ dysfunction following transient ischemic insults. Although numerous interventions have been found effective to reduce IR injury in preclinical models, none of these therapies have been successfully translated to the clinical setting. In the context of the persistent translational gap, we systematically investigated the mechanisms implicated in IR injury using kidney donation and transplantation as a clinical model of IR. Whilst our results do not implicate traditional culprits such as reactive oxygen species, complement activation or inflammation as triggers of IR injury, they reveal a clear metabolic signature for renal IR injury. This discriminatory signature of IR injury is consistent with a post-reperfusion metabolic paralysis and involves high-energy phosphate depletion, tricarboxylic acid cycle defects, and a compensatory activation of catabolic routes. Against this background, the picture emerges that clinical IR injury is driven by reductive stress. In this article, we therefore wish to elaborate on the processes contributing to reductive stress in the context of clinical IR injury and provide a better insight in potential clinical therapeutic strategies that might be helpful in restoring the redox balance.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149539"},"PeriodicalIF":3.4,"publicationDate":"2025-01-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143015587","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Purification and characterization of recombinant human mitochondrial proton-pumping nicotinamide nucleotide transhydrogenase","authors":"Sangjin Hong ,&nbsp;Simone Graf ,&nbsp;Christoph von Ballmoos ,&nbsp;Robert B. Gennis","doi":"10.1016/j.bbabio.2025.149540","DOIUrl":"10.1016/j.bbabio.2025.149540","url":null,"abstract":"<div><div>The human mitochondrial nicotinamide nucleotide transhydrogenase (NNT) uses the proton motive force to drive hydride transfer from NADH to NADP⁺ and is a major contributor to the generation of mitochondrial NADPH. NNT plays a critical role in maintaining cellular redox balance. NNT-deficiency results in oxidative damage and its absence results in familial glucocorticoid deficiency. Recently it has also become clear that NNT is a tumor promoter whose presence in mouse models of non-small cell lung cancer results in enhanced tumor growth and aggressiveness. The presence of NNT mitigates the effects of oxidative stress and facilitates cancer cell proliferation, suggesting NNT-inhibition as a promising therapeutic strategy. The human NNT is a homodimer in which each subunit has a molecular weight of 114 kDa and 14 transmembrane spans. Here we report on the development of a system for isolating full-length recombinant human NNT using <em>Escherichia coli</em>. The purified enzyme is catalytically active, and the enzyme reconstituted into proteoliposomes pumps protons and generates a proton motive force capable of driving ATP synthesis by <em>E. coli</em> ATP synthase. The recombinant human NNT will facilitate structural and biochemical studies as well as provide a useful tool to develop and characterize potential anti-cancer therapeutics.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149540"},"PeriodicalIF":3.4,"publicationDate":"2025-01-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143015687","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":"Mutational interference with oligomerization properties of OCP-related apo- and holoproteins studied by analytical ultracentrifugation","authors":"Anna Marta Koczula ,&nbsp;Nils Cremer ,&nbsp;Marcus Moldenhauer ,&nbsp;Nikolai N. Sluchanko ,&nbsp;Eugene G. Maksimov ,&nbsp;Thomas Friedrich","doi":"10.1016/j.bbabio.2025.149538","DOIUrl":"10.1016/j.bbabio.2025.149538","url":null,"abstract":"<div><div>In this study, the oligomerization pattern of apo- and holoforms of the Orange Carotenoid Protein (OCP) was examined under different conditions such as photoactivation state, concentration, and carotenoid embedment using analytical ultracentrifugation. Furthermore, studies were conducted on OCP constructs carrying point mutations of amino acid residues affecting OCP oligomerization. Our findings reveal that the concentration-dependent dimerization of dark-adapted OCP holoprotein from <em>Synechocystis</em> sp. PCC 6803 can be effectively prevented by the R27L mutation in the OCP-NTD. By introducing the E258R mutation (also in conjunction with R27L) into the OCP-CTD, monomeric OCP apoprotein can be obtained. Additionally, the holoprotein of the dark-adapted OCP-R27L/E258R variant was monomeric, and, supported by size-exclusion chromatography experiments, the photoactivated form of the OCP-R27L/E258R variant was monomeric as well. This variant, which does not oligomerize in either photocycle state, returns from the photoactivated to the dark-adapted state at a significantly faster rate than the OCP wild-type and the R27L mutant thereof. These observations also highlight the crucial interdependence between OCP dimerization in both photocycle states, the lifetime of the photoactive state of OCP, and the kinetics of the OCP photocycle.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149538"},"PeriodicalIF":3.4,"publicationDate":"2025-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143015682","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"ADP-inhibited structure of non-catalytic site-depleted FoF1-ATPase from thermophilic Bacillus sp. PS-3","authors":"Ren Kobayashi ,&nbsp;Astuki Nakano ,&nbsp;Kaoru Mitsuoka ,&nbsp;Ken Yokoyama","doi":"10.1016/j.bbabio.2025.149536","DOIUrl":"10.1016/j.bbabio.2025.149536","url":null,"abstract":"<div><div>The F₁ domain of F_oF₁-ATP synthases/ATPases (F_oF₁) possesses three catalytic sites on the three αβ interfaces, termed α_Eβ_E, α_Dβ_D, and α_Tβ_T, located mainly on the β subunits. The enzyme also has three non-catalytic ATP-binding sites on the three αβ interfaces, located mainly on the α subunits. When ATP does not bind to the non-catalytic site, F_oF₁ becomes significantly prone to ADP inhibition, ultimately resulting in the loss of ATPase activity. However, the underlying mechanism of ADP inhibition remains unclear. Here, we report the cryo-EM structure of the non-catalytic site-depleted (<em>ΔNC</em>) F_oF₁ from thermophilic Bacillus sp. PS-3, which completely lacks the ability to bind ATP (and ADP) upon transitioning to the ADP-inhibited form. The structure closely resembled the 81° rotated structure of the wild-type F_oF₁, except for minor movements in the C-terminal region of the α subunit. In this structure, unlike the wild-type enzyme, the catalytic site at α_Dβ_D, responsible for ATP hydrolysis, was occupied by ADP-Mg, with the absence of Pi. Furthermore, the catalytic site at α_Eβ_E, where ATP enters the F₁ domain during steady-state catalysis, is occupied by ADP, seemingly impeding further ATP binding to the enzyme. The structure suggests that the ADP-inhibited form of the F₁ domain is more likely due to differences in the nucleotide-binding states at the catalytic sites rather than structural differences.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149536"},"PeriodicalIF":3.4,"publicationDate":"2025-01-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142958114","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 mitochondriotropic antioxidants AntiOxBEN2 and AntiOxCIN4 are structurally-similar but differentially alter energy homeostasis in human skin fibroblasts","authors":"José Teixeira ,&nbsp;Sofia Benfeito ,&nbsp;Rodrigo Carreira ,&nbsp;André Barbosa ,&nbsp;Ricardo Amorim ,&nbsp;Ludgero C. Tavares ,&nbsp;John G. Jones ,&nbsp;Nuno Raimundo ,&nbsp;Fernando Cagide ,&nbsp;Catarina Oliveira ,&nbsp;Fernanda Borges ,&nbsp;Werner J.H. Koopman ,&nbsp;Paulo J. Oliveira","doi":"10.1016/j.bbabio.2025.149535","DOIUrl":"10.1016/j.bbabio.2025.149535","url":null,"abstract":"<div><div>Mitochondrial dysfunction and increased reactive oxygen species (ROS) generation play an import role in different human pathologies. In this context, mitochondrial targeting of potentially protective antioxidants by their coupling to the lipophilic triphenylphosphonium cation (TPP) is widely applied. Employing a six‑carbon (C₆) linker, we recently demonstrated that mitochondria-targeted phenolic antioxidants derived from gallic acid (AntiOxBEN₂) and caffeic acid (AntiOxCIN₄) counterbalance oxidative stress in primary human skin fibroblasts by activating ROS-protective mechanisms. Here we demonstrate that C₆-TPP (but not AntiOxBEN₂ and AntiOxCIN₄) induce cell death in human skin fibroblasts. This indicates that C₆-TPP cytoxocity is counterbalanced by the antioxidant moieties of AntiOxBEN₂ and AntiOxCIN₄. Remarkably, C₆-TPP and AntiOxBEN₂ (but not AntiOxCIN₄) induced a glycolytic switch, as exemplified by a reduced cellular oxygen consumption rate (OCR), increased extracellular acidification rate (ECAR), elevated extracellular lactate levels, and higher protein levels of glucose transporter 1 (GLUT-1). This switch involved activation of AMP-activated protein kinase (AMPK) and fully compensated for the loss in mitochondrial ATP production by sustaining cellular ATP content. When glycolytic switch induction was prevented (<em>i.e.</em> by using a glucose-free, galactose-containing medium), AntiOxBEN₂ induced cell death whereas AntiOxCIN₄ did not. We conclude that, despite their similar chemical structure and antioxidant capacity, AntiOxBEN₂ and AntiOxCIN₄ display both common (redox-adaptive) and specific (bioenergetic-adaptive) effects.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149535"},"PeriodicalIF":3.4,"publicationDate":"2025-01-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142958120","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":"Interplay of acidic residues in the proton channel of E. coli cytochrome bd-I oxidase to promote oxygen reduction and NO release","authors":"Raaif Siddeeque ,&nbsp;Lucia Heger ,&nbsp;Jan Kägi ,&nbsp;Thorsten Friedrich ,&nbsp;Frédéric Melin ,&nbsp;Petra Hellwig","doi":"10.1016/j.bbabio.2025.149537","DOIUrl":"10.1016/j.bbabio.2025.149537","url":null,"abstract":"<div><div>The reduction of oxygen to water is crucial to life under aerobic conditions. Cytochrome <em>bd</em> oxidases perform this reaction with a very high oxygen affinity. Members of this protein family are solely found in prokaryotes and some archaea playing an important role in bacterial virulence and antibiotic resistance. Here, we combine mutagenesis, electrocatalysis, nitric oxide binding and release experiments as well as FTIR spectroscopy to demonstrate that proton delivery to the active site is essentially rate limiting in Cyt <em>bd-</em>I electrocatalysis. D58 and D105 of subunit CydB are crucial residues in this proton path and communicate via a hydrogen bond network. Oxygen reduction depends on proton delivery to the active site, which also influences NO release.</div></div>","PeriodicalId":50731,"journal":{"name":"Biochimica et Biophysica Acta-Bioenergetics","volume":"1866 2","pages":"Article 149537"},"PeriodicalIF":3.4,"publicationDate":"2025-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142958161","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}