BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS生物化学与生物物理学学报-生物能学
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS(英文缩写 BBA-BIOENERGETICS),ISSN 0005-2728,eISSN 1879-2650,中文译名:生物化学与生物物理学学报-生物能学 是一本学术期刊。本页汇总该期刊的最新影响因子、分区信息以及最新收录于 PubMed 的文献,帮助您快速了解期刊全貌。
发文量统计区间：2025-09-27 至 2026-09-27，按本站收录文献的发表日期统计。
期刊介绍
历年影响因子趋势
| JCR 数据年份 | 影响因子 | JCR 分区 |
|---|---|---|
| 2021 | 4.428 | Q2 |
| 2022 | 4.300 | Q1 |
| 2023 | 3.400 | Q1 |
| 2024 | 2.700 | Q2 |
| 2025 | 2.600 | Q3 |
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 最新收录文献
-
1. Adenine nucleotide-dependent inhibition of permeability transition pore: adenine nucleotide translocase and other players.
PMID:日期:2026-11-01Changes in the level and the ratio of adenine nucleotides (AN) are a common consequence of ischemia, which can promote mitochondrial permeability transition pore (mPTP) opening and cell death upon reperfusion. However, the mechanism of AN-dependent mPTP inhibition is not entirely clear. Here we studied the effects of inorganic phosphate, Mg, as well as the inhibitors of adenylate translocase (ANT) and FoF-ATP synthase (F-ATPase) on the AN-dependent mPTP suppression and AN turnover mediated by a short Ca-dependent mitochondrial carrier (SCaMC). Also, we indirectly assessed the contribution of Ca buffering by AN to mPTP suppression. We found that, at near-physiologic concentrations, AN suppressed mPTP opening (swelling) and increased the Ca-retention capacity much stronger than the ANT inhibitor bongkrekic acid (BA). Inorganic phosphate (Pi) and Mg modulated the protective effect of AN. In solution, AN were an incomparably weaker Ca buffer than matrix Pi. AN preserved the capability to suppress mPTP opening in the presence of both BA and carboxyatractyloside (CATR). The sensitivity of AN-dependent mPTP suppression to CATR decreased with a decrease in the Pi level. Mg and BA, in contrast to CATR, partially inhibited the SCaMC-mediated AN turnover. The analysis of these and the earlier obtained data allowed us to propose a new mechanism of AN-dependent mPTP suppression: the coordinated ANT- and SCaMC-mediated AN turnover, which fine-tunes the Pi, Ca, and H ratios in the matrix for efficient Ca sequestration. The mechanism does not require ANT stabilization in any conformation, allosteric regulators, and the formation of AN-Ca-Pi complexes.
-
2. Disease-mutations perturb proton transfer reactions in respiratory complex I.
PMID:日期:2026-11-01Respiratory Complex I powers oxidative phosphorylation by a long-range proton-coupled electron transfer (PCET) reaction, with mutations linked to more than half of all human mitochondrial disorders. Yet, the molecular principles underlying the functional impairment remain difficult to test, as most mutations impede both the proton pumping and oxidoreductase activities due to the tightly coupled PCET process. Here, we probe how key disease mutations in the terminal ND5 subunit (NuoL/Nqo12), linked to the development of Leigh's syndrome (LS) and LHON/MELAS (F124L, M252T, D393N), affect the proton transport activity within the dissected antiporter module Nqo12. All constructs result in fully folded antiporter modules, with the introduced substitutions showing enhanced proton conduction rates across the proteoliposome membranes relative to the wild type module. Our molecular dynamics simulations reveal that the mutations perturb the internal water network and ion-pair dynamics that are central for the long-range PCET activity in Complex I. Taken together, we suggest that the mitochondrial disease mutations alter the redox-driven proton pumping activity of Complex I by perturbing the function of local proton gates, and result in an uncontrolled proton translocation across the antiporter module. The molecular consequences of disease mutations are discussed in the context of the proposed pumping mechanism.
-
3. {"_":"Biochemical and spectroscopic characterization of photocomplexes from the extremely halophilic purple sulfur bacterium, Halorhodospira halophila strain SL1.","sup":["T"]}
PMID:日期:2026-11-01The purple sulfur phototrophic bacterium Halorhodospira (Hlr.) halophila type strain SL1 (= DSM244) is among the most halophilic bacteria known and has been used as a model for exploring the osmoadaptive and photosynthetic strategies that enable phototrophs to thrive in hypersaline environments. Here we report the isolation and characterization of four photocomplexes from this organism: a conjoined core and peripheral light-harvesting complex (LH1-LH2), a light-harvesting-reaction center complex (LH1-RC), and two individual light-harvesting complexes, LH1-only (LH1-B880) and LH2-only. Although the LH1-LH2 and LH1-RC complexes displayed similar spectral features to those of their corresponding complexes from Hlr. halophila strain BN9622, the LH2 B850 absorption maxima in both LH1-LH2 and LH2-only complexes of strain SL1 differed from those of strain BN9622. This difference could be linked to the substitution of a key amino acid residue in the strain SL1 LH2 α-polypeptides. The LH1-B880 complex from strain SL1 was unstable in the absence of salts and converted to a unique intermediate species with an absorption maximum at 850 nm. These findings are compared with those from strain BN9622 and discussed with respect to the electrostatic charge interactions that maintain thermal and spectral stabilities of these photocomplexes and underlie the adaptation of halophilic phototrophs to their hypersaline habitats.
-
4. {"_":"Na-translocating oxaloacetate decarboxylase from Vibrio cholerae: the functional tautomeric form of the substrate and the proton pathways in catalysis.","sup":["+"]}
PMID:日期:2026-11-01Membrane-bound decarboxylases couple carboxylic acid decarboxylation to the transport of Na ions out of prokaryotic cells. The molecular mechanism of decarboxylase action is not yet known, which contrasts with the progress achieved in studying other primary ion pumps. Measuring decarboxylase activity is complicated by slow keto-enol tautomerization of the substrates during the assay. We found that HEPES exhibits anomalously high efficiency as a general acid catalyst for CH bond formation during the enol-to-ketone conversion of oxaloacetate. Accordingly, the addition of HEPES to the assay medium eliminated the contribution of tautomerization rate to measured decarboxylation rate. Using the dependence of oxaloacetate tautomerization rate and equilibrium on solvent properties and pH, we established that only the keto form of oxaloacetate is converted by Vibrio cholerae oxaloacetate decarboxylase. Steady-state kinetic measurements did not reveal cooperativity in oxaloacetate conversion and Na binding. The effects of ionophores (CCCP, valinomycin, and ETH157) on proton transport in pyranine-loaded membrane vesicles prepared from V. cholerae cells indicated that the proton required for the conversion of oxaloacetate to pyruvate is taken up from the cytoplasmic side of the membrane. Furthermore, the effects suggested that ΔpH generation is caused by secondary electrophoretic proton transport in exchange for Na. These findings advance our understanding of the molecular mechanism of the decarboxylation-supported Na transport in bacteria.
-
5. Size-dependent fluorescence kinetics reveal contributions of intrinsic quenching and singlet-triplet annihilation during LHCII aggregation.
PMID:日期:2026-11-01Aggregation of the main antenna complex of higher plants, Light-Harvesting Complex II (LHCII), is widely used as an in-vitro model for energy-dependent quenching (qE), yet fluorescence reduction in aggregates is frequently interpreted without a quantitative separation of intrinsic quenching from excitation-induced annihilation. Here, we address this ambiguity by directly correlating aggregate size, concentration, steady-state fluorescence intensity, and decay kinetics during controlled, incremental aggregation of isolated LHCII. By combining fluorescence correlation spectroscopy (FCS) with time-correlated single-photon counting (TCSPC) in a unified experimental framework, we monitored structural and photophysical changes in real time as detergent removal drives biphasic aggregation. We quantified the aggregate composition from the particle concentrations, enabling direct scaling of the absorption cross-section with aggregate size. The average fluorescence lifetime decreased semi-logarithmically with increases in hydrodynamic radius, whereas steady-state fluorescence intensities deviated strongly from this trend. Intensity-dependent measurements and steady-state kinetic modeling reveal that singlet-triplet annihilation (STA) emerges at moderate excitation intensities and rapidly becomes the dominant contributor to fluorescence quenching, even for relatively small aggregates. In contrast, intrinsic quenching increases more gradually with aggregate size. By quantitatively disentangling intrinsic excitation quenching from annihilation processes, this work demonstrates that STA can govern the apparent photophysical response of aggregated LHCII across excitation regimes commonly considered non-annihilating. The size-dependent mechanistic framework presented here provides a basis for distinguishing intrinsic quenching from annihilation effects in aggregation-based studies of photosynthetic antenna complexes.
-
6. Biosynthesis of C-phycocyanin trimers.
PMID:日期:2026-11-01Phycobiliproteins, particularly C-phycocyanin (CPC), serve as major light-harvesting complexes in cyanobacteria, exhibiting high efficiency in light-harvesting and energy transfer. Currently, the easy and large-scale acquisition of functional CPC remains a major challenge, primarily due to the requirement for precise, sequential covalent attachment of multiple phycocyanobilin (PCB) chromophores. In this study, by using a dual-promoter (T7 and araBAD) system to control the sequential binding of two PCB chromophores to β82 and β153, we successfully achieved the biosynthesis of β-CPC (λ = 605 nm, λ = 644 nm) in E. coli, which can transfer energy from the β153-PCB to the β82-PCB. The assembly of α-CPC with PCB-β82, PCB-β153, and PCB-β under identical conditions indicates that only PCB-β, which covalently binds the two PCB chromophores, can assemble with α-CPC to form a complete CPC trimer (λ = 617 nm, λ = 646 nm). The structure of the assembled trimer reveals that it adopts a typical phycobiliprotein fold, with multiple chromophores precisely arranged, exhibiting features highly similar to those of native CPC. Furthermore, we established a biosynthetic pathway for CPC trimers in E. coli. This system provides a powerful tool for engineering phycobiliproteins with various light-harvesting and energy transfer properties, facilitating future studies on artificial photosynthesis, light-harvesting antenna design, and the fundamental mechanisms of excitation energy transfer.
-
7. Cryo-EM structure of photosystem II D1-V185T mutant from Thermosynechococcus vestitus.
PMID:日期:2026-11-01Photosystem II (PSII) catalyzes water oxidation into electrons, protons and dioxygen at its catalytic center, a MnCaO cluster, utilizing light energy. An amino acid residue D1-V185 in the D1 protein is located close to the MnCaO cluster, and plays a critical role in its catalytic function. In this research we purified PSII dimers from a D1-V185T mutant of Thermosynechococcus vestitus and analyzed its structure using low-damage cryo-electron microscopy (cryo-EM) at a resolution of 1.88 Å. The results revealed the presence of multi-conformations at the mutation site. Unlike the wild-type valine, which does not allow water molecules to be able to form hydrogen-bonds with it, both conformations of the mutant formed hydrogen bonds with nearby water molecules, which leads to rearrangement of the hydrogen bond networks in the O1 and Cl-1 channels. In conformation-A, the mutated Thr residue forms a hydrogen bond with a water molecule W6, which creates a new channel that bypasses the original O1 channel. Due to the hydrophilic OH group of Thr, the side-chain of D1-Glu189 was attracted and shifted toward the mutant Thr residue. In conformation-B, it forms a hydrogen bond with a water molecule W9 in the Cl-1 channel, bringing W9 closer and thereby disrupting the hydrogen bond network of the Cl-1 channel. In addition, multi-conformations of D2-K317, which is a ligand of Cl-1, were found in the mutant. These changes alter the environment surrounding the Cl-1 ion and MnCaO, thereby affecting the PSII water-oxidation activity.
-
8. PGR5 is needed for regulation of ATP synthase in plant chloroplasts.
PMID:日期:2026-11-01Regulation of proton motive force (pmf) via ATP synthase activity is a critical mechanism by which photosynthetic organisms maintain redox homeostasis and control the activation and inactivation of photoprotective responses under fluctuating light conditions. Here, we used time-resolved electrochromic shift measurements to investigate pmf dynamics in the C model plant Arabidopsis thaliana and the C model grass Setaria viridis. Our results reveal that ATP synthase is dynamically regulated during light fluctuations, but in Arabidopsis this regulation could not be explained by the established light-induced reduction of the CF₁γ subunit by thioredoxins, suggesting alternative control mechanisms. The PROTON GRADIENT REGULATION 5 (PGR5) protein, previously proposed to facilitate cyclic electron transport (CET) in plants and algae, also has a potential role in regulation of ATP synthase. We therefore investigated pmf dynamics, cytochrome f redox changes, and linear and cyclic PSI electron transport rates in WT and pgr5 knock-out mutants and revealed that while PGR5 was not required for CET, it was needed for downregulating ATP synthase under high irradiance in both species. Furthermore, in Arabidopsis disturbance of thiol redox regulation by addition of N-ethylmaleimide resulted in downregulation of ATP synthase conductivity in WT but not in pgr5 mutants, and PGR5 interacted with CF₁γ in planta. We suggest that PGR5 functions as a conserved thiol redox state dependent inhibitor of chloroplast ATP synthase under high light, contributing to pmf retention and photoprotection.
-
9. Expansion microscopy visualizes the photosystem distribution in Synechocystis cells.
PMID:日期:2026-11-01Photosynthesis in cyanobacteria relies on light capture by photosystem I (PSI), photosystem II (PSII) and the phycobilisome (PBS). Although these complexes are generally considered to be intermixed within the thylakoid membrane, several studies have suggested the presence of PSI- or PSII/PBS-enriched microdomains that may depend on environmental conditions. Here we applied cryo-Expansion Microscopy (cryo-ExM) to dark-adapted Synechocystis sp. PCC 6803 cells and achieved nanoscale resolution of thylakoid compartments and associated protein complexes. Cells were cryofixed, rehydrated at room temperature and physically expanded in a swellable hydrogel. By expanding cells 5.5-fold, we resolved individual thylakoid compartments in intact cells using confocal microscopy. Furthermore, immunolabeling allowed simultaneous localization of PSI, PSII and PBS within the expanded thylakoid network. Overall PSI, PSII, and PBS signals showed similar spatial distributions. However, PBS was excluded from the neck region between dividing cells, while PSI and PSII were present. These results establish cryo-ExM as a powerful method for visualizing cyanobacterial thylakoid membranes and mapping the distribution of key photosynthetic complexes, thereby complementing existing approaches for dissecting the spatial organization of photosynthesis.
-
10. Mitochondrial dysfunction redirects proton transport and energy homeostasis in Saccharomyces cerevisiae under variable pH and glucose conditions.
PMID:日期:2026-11-01Mitochondrial function is crucial for the regulation of energy metabolism, proton homeostasis, and stress adaptation in Saccharomyces cerevisiae. This study demonstrates the role of mitochondria in modulating cellular responses to varying extracellular pH (3.0, 5.0, 6.5) and glucose availability (0.5%, 2%). Results indicate that mitochondrial deficiencies in Δhap4 and ρ mutants selectively impair growth under acidic pH and 0.5% glucose conditions, whereas wild-type cells maintain pH-independent growth. Mitochondrial impairment redistributes intracellular H homeostasis regulation to plasma membrane and cytosolic H-ATPases in a glucose- and pH-dependent manner, with ρ cells exhibiting maximal reliance on non-mitochondrial ATPases. The N, N'- dicyclohexylcarbodiimide (DCCD)-sensitive J scales inversely with glucose availability, reflecting energy demand under nutrient limitation and acid stress. ρ cells exhibit the highest alcohol dehydrogenase activity to regulate the redox balance in response to non-functional mitochondria. The highest total H-ATPase activity measured in ρ cells at pH 6.5 and 0.5% glucose conditions, combined with proton flux data, indicates the upregulation of plasma membrane and cytosolic ATPases activity for maintaining proton motive force and intracellular pH due to a complete loss of FF-ATPase contribution. These results pave the way for the construction of robust S. cerevisiae yeast strains to varying glucose and extracellular pH conditions.