ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS生物化学与生物物理档案
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS(英文缩写 ARCH BIOCHEM BIOPHYS),ISSN 0003-9861,eISSN 1096-0384,中文译名:生物化学与生物物理档案 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：2025-11-01 至 2026-10-31，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 | 4.114 | Q2 |
| 2022 | 3.900 | Q1 |
| 2023 | 3.800 | Q1 |
| 2024 | 3.000 | Q2 |
| 2025 | 3.500 | Q2 |
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 最新收录文献
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2. Ablation of phospholipase D1 mitigates obesity-mediated pancreatic edema in a mouse model of acute pancreatitis.
PMID:日期:2026-09-29Acute pancreatitis (AP) is a multifactorial inflammatory disease driven by premature activation of pancreatic digestive enzymes, with obesity representing a major risk factor for increased disease severity and systemic complications. Phospholipase D (PLD) regulates inflammatory signaling, and expression of its classical isoform, PLD1, is upregulated during AP; however, its role in obesity-associated AP remains poorly defined. In this study, we investigated the contribution of PLD1 to high-fat diet (HFD)-exacerbated AP in vivo. Male and female wild-type (WT) and PLD1-deficient (Pld1) mice were fed a control diet (CD) or HFD for 18 weeks, followed by cerulein-induced AP. HFD feeding increased body weight, fat mass, and serum leptin levels in both WT and Pld1 mice, while serum adiponectin was significantly reduced in WT-HFD mice. Importantly, HFD significantly exacerbated pancreatic edema and increased pancreatic weight in WT mice; these effects were attenuated by PLD1 ablation. Exploratory transcriptomic and targeted gene expression analyses revealed that PLD1 deficiency promoted survival and regenerative gene expression programs while suppressing HFD-induced pancreatic Il-1β expression. Together, these findings identify PLD1 as a modulator of obesity-associated pancreatic injury and inflammation and suggest that targeting PLD1 may represent a promising therapeutic strategy to mitigate HFD-driven exacerbation of AP.
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3. Activation of Cu(II)-reducing ability of monoamine neurotransmitters triggered by amyloid-β fibrillization.
3. 淀粉样β蛋白纤维化触发单胺神经递质铜(II)还原能力的激活PMID:日期:2026-09-26The reduction of Cu(II) to Cu(I) in oxidative extracellular environments contributes to oxidative stress because the reoxidation of Cu(I) back to Cu(II) generates reactive oxygen species. Monoamine neurotransmitters such as serotonin (5-HT) and dopamine (DA) possess Cu(II)-reducing ability and coexist with copper ions near the synapse, suggesting that they may serve as potential mediators of oxidative stress. The neurotoxicity of aggregated amyloid-β peptide (Aβ) observed in the brains of Alzheimer's disease patients is thought to arise from oxidative stress induced by complex formation of Aβ with redox-active metal ions. However, the absence of apparent Cu(II)-reducing activity in Aβ suggests the involvement of other reducing agents in the generation of oxidative stress. In this study, we examined the effects of Aβ on the redox reactions between copper and monoamine neurotransmitters 5-HT and DA. The Cu(II)-reducing activities of both neurotransmitters, together with the accompanying production of hydrogen peroxide, were inhibited by either unfibrillized Aβ or non-amyloidogenic Aβ, whereas fibrillized Aβ enhanced them. Canonical small-molecule Cu(II) ligands, such as l-histidine, diminished these activities, whereas Cu(I) chelators exerted an enhancing effect. These findings suggest that the activation of monoamine-mediated copper reduction by fibrillized Aβ may be attributable to the Cu(I)-binding capability that is absent in the monomeric form. This study provides a partial mechanistic basis for the causal link between Aβ aggregation and the onset of Alzheimer's disease.
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4. The mucosal redox gateway for dietary iron absorption: integrating gastrointestinal mucus, Fe(II)/Fe(III) speciation and ligand-centred valence tautomerism.
PMID:日期:2026-09-22Non-haem dietary iron reaches the duodenum as a dynamic mixture of Fe(III) and Fe(II) complexes whose solubility and exchange kinetics are strongly influenced by pH, reductants, proteases, lipases, carbohydrases, and competing ligands. Canonical models place ferrireduction by duodenal cytochrome b and Fe(II) transport by divalent metal transporter 1 at the centre of absorption, but usually treat gastrointestinal mucus as a passive diffusion barrier. Evidence that mucins bind iron and other metal cations suggests a more active role. This review integrates established epithelial transport biology with mucin coordination chemistry and proposes a mucosal redox gateway: gastric and duodenal mucus transiently captures iron, suppresses premature hydrolysis and precipitation, and presents an exchangeable iron pool to the apical surface. Within this pool, Fe(III)/Fe(II) interconversion could be coupled to reversible oxidation-state changes in mucin-associated or low-molecular-mass ligands. We use the term ligand-centred valence tautomerism narrowly for an intracomplex redox equilibrium and distinguish this testable chemical hypothesis from the established phenomenon in discrete coordination compounds. The model predicts spatial gradients in iron speciation across mucus, redox- and pH-dependent exchange with mucin, and altered epithelial flux after selective modification of mucin functional groups. It provides a framework for explaining why ascorbate, gastric acidity, inflammation, mucus composition and competing metals influence iron bioavailability. Direct validation will require operando X-ray absorption spectroscopy, Mössbauer or electron paramagnetic resonance measurements, redox-resolved mass spectrometry and isotope-tracer transport in human mucus-organoid systems.
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5. Nitro-arachidonic acid inhibits prostaglandin endoperoxide H synthase 2 through histidine-mediated heme-binding conformational perturbation.
PMID:日期:2026-09-21Prostaglandin endoperoxide H synthase (PGHS) is a heme-containing enzyme that catalyzes the conversion of arachidonic acid (AA) into prostaglandin H. The anti-inflammatory mediator nitro-arachidonic acid (NOAA) has been identified as a potent inhibitor of both PGHS1 and PGHS2 isoforms. While this inhibition involves the displacement of the essential heme prosthetic group from the active site, the underlying molecular mechanism remains incompletely elucidated. Herein, we investigated the inhibitory action of NOAA against murine PGHS2 (mPGHS2) using site-directed mutagenesis targeting the peroxidase (POX) active sites, combined with kinetic analysis and mass spectrometry. NOAA dose-dependently inactivates both COX and POX activities. Mutations of key histidine residues -H386A, H207A, and H388F- abrogated this inactivation in WT-mPGHS2. The apoenzyme incubated with NOAA and then reconstituted with heme, as well as the holoenzyme inhibited by the addition of NOAA and then reconstituted with heme, did not recover their enzymatic activity. Despite the potential for NOAA to modify residues that coordinate the heme group, we were unable to detect covalent nitroalkylation at these sites, suggesting that NOAA induces heme release through a non-covalent, irreversible mechanism. Nano-scale differential scanning fluorimetry (nanoDSF) confirmed that NOAA triggers a selective disruption of heme stabilization within the protein structure, a process hindered by mutations at His-207, His-386, and His-388. These results support a model in which NOAA interacts with the POX active site, with histidine residues playing a crucial role in the interaction that triggers heme displacement. These insights enhance our understanding of the NOAA mechanism of action and underscore its potential as a scaffold for targeted anti-inflammatory drug development.
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6. Mechanistic insights into nicotine oxidation by FAD-dependent nicotine dehydrogenase from Pseudomonas sp. HZN6.
6. 假单胞菌HZN6中FAD依赖性尼古丁脱氢酶催化尼古丁氧化的机制研究PMID:日期:2026-09-21Nicotine dehydrogenase from Pseudomonas sp. HZN6 (Nox) is a flavin-dependent enzyme that specifically catalyzes (S)-nicotine degradation through a relatively simple mechanism, making it a promising candidate for biotechnological applications. Although enzyme engineering has extensively targeted the oxidative half-reaction, key mechanistic details of the reductive half-reaction, particularly substrate oxidation, remain unclear. In this study, a three-dimensional model of the Nox-FAD-nicotine complex was constructed using AlphaFold in combination with molecular docking. This model enabled identification of putative catalytically relevant residues, specifically interaction network formed by residues E245, Y210, and Y214, located near the pyrrolidine nitrogen of (S)-nicotine. Site-directed mutagenesis combined with rapid kinetic analysis revealed that disruption of this network significantly decreased the rate of electron transfer from (S)-nicotine to FAD in the reductive half-reaction, as well as substrate binding affinity. Notably, these mutations did not affect the FAD oxidation with molecular oxygen during the oxidative half-reaction, which remains the rate-determining step. Consequently, the overall (S)-nicotine consumption activity was unaffected, even in variants where hydrogen-bonding capacity was completely abolished. These findings indicate that these residues are not strictly required as essential catalytic bases for (S)-nicotine oxidation. Instead, the active-site environment primarily facilitates proper substrate positioning and structural organization within the active site, thereby facilitating efficient catalysis.
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7. Elucidation of D-alanine biosynthetic pathways in the hyperthermophiles: Characterization of alanine racemase from Thermus thermophilus and the structure and dual physiological functions of lysine racemase from Thermotoga maritima.
7. 嗜热微生物中D-丙氨酸生物合成途径的阐明：嗜热栖热菌丙氨酸消旋酶的表征以及海栖热袍菌赖氨酸消旋酶的结构与双重生理功能PMID:日期:2026-09-21The hyperthermophilic bacterium Thermotoga maritima contains a peptidoglycan comprising D-alanine, D-glutamate, and D-lysine. We have previously identified the biosynthetic pathways of D-lysine and D-glutamate; however, the biosynthetic pathway of D-alanine is unclear in T. maritima. The present study elucidated the D-alanine biosynthetic pathway in T. maritima, following the characterization of the TTHA0062 activity, constructed a TTHA0062 (encoding alanine racemase)-deficient Thermus thermophilus (ΔTTHA0062) strain. TTHA0062 exhibited the racemase activity toward 10 amino acids including Ala, and the catalytic efficiency of L-alanine was 2-fold higher than that of D-alanine. Regarding the T. maritima genes introduced into the genome of the ΔTTHA0062 strain, TM1597 (lysine racemase) completely restored the growth, TM1270 (multifunctional enzyme) resulted in partial restoration, whereas TM0831 (D-amino acid aminotransferase) had no effect, suggesting that TM1597 and TM1270 are involved in D-alanine biosynthesis in T. maritima. Furthermore, we determined the crystal structure of TM1597 in the internal aldimine form, in which pyridoxal 5'-phosphate (PLP) forms a Schiff base linkage with the active site residue Lys36, and revealed the residues crucial for the catalytic reaction by TM1597 mutational analysis.
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8. A matter of balance: Heme oxygenase-1 at the crossroads of healthy and pathological aging.
8. 平衡之事：血红素加氧酶-1在健康衰老与病理性衰老交叉点上的作用PMID:日期:2026-09-20Increasing life expectancy has led to a growing prevalence of age-related disorders, including dementia, cardiovascular disease, frailty, osteoporosis, sarcopenia, and cancer. Heme oxygenase-1 (HO-1), a stress-inducible enzyme that degrades heme into carbon monoxide (CO), biliverdin which is then reduced to bilirubin by the biliverdin reductase enzyme, and iron, has emerged as a key regulator of several hallmarks of aging, including oxidative stress, inflammation, autophagy, mitochondrial dysfunction, and cellular senescence. This review evaluates age-associated changes in HO-1 expression across major organs and examines the roles of HO-1 and its metabolites in age-related diseases, with particular emphasis on dementia and cardiovascular disorders. Current evidence suggests that the biological effects of HO-1 depend not only on expression level but also on temporal regulation, tissue specificity, and the balance between protective and deleterious downstream pathways. Future research should focus on defining physiological and therapeutic ranges of HO-1 activity in different tissues, sexes, and stages of aging, while clarifying the distinct contributions of CO, bilirubin, and iron metabolism. Such studies may enable precision-medicine approaches that harness HO-1 modulation to promote healthy aging and prevent age-related diseases.
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9. ROS-activated SHP-1 signaling underlies artesunate-mediated inhibition of EMT and STAT3-Driven prostate cancer progression.
9. ROS激活的SHP-1信号通路是青蒿琥酯介导抑制EMT和STAT3驱动的前列腺癌进展的基础PMID:日期:2026-09-19Constitutive activation of signal transducer and activator of transcription 3 (STAT3) is a hallmark of prostate cancer (PC) progression. Here, we investigated the anticancer effects of artesunate (ART) and its underlying mechanisms in PC. ART selectively reduced the viability of PC cells with minimal toxicity toward normal prostate cells by inducing apoptosis, as evidenced by increased sub-G1 accumulation, Annexin V/propidium iodide (PI)-positive cells, and DNA fragmentation. These effects were mediated by reactive oxygen species (ROS), as glutathione (GSH) and N-acetyl-l-cysteine (NAC) significantly reversed ART-induced cytotoxicity. ART also depleted intracellular GSH and reduced superoxide dismutase (SOD) expression, thereby enhancing oxidative stress. Inhibition of STAT3 by ART was reversed by sodium orthovanadate, implicating protein tyrosine phosphatases (PTPs) in this process. ART downregulated anti-apoptotic B-cell lymphoma-2 (Bcl-2) family proteins, suppressed C-X-C motif chemokine ligand 12 (CXCL12)-induced migration, and inhibited epithelial-mesenchymal transition (EMT) through ROS-dependent activation of Src homology region 2 domain-containing phosphatase-1 (SHP-1). In vivo, ART significantly inhibited prostate tumor xenograft growth, reduced oncogenic protein expression in tumors, and lowered serum interleukin-6 (IL-6) and tumor necrosis factor-α (TNF-α) levels. Collectively, ART suppresses PC growth, survival, migration, and EMT by targeting the STAT3 and ROS/SHP-1 signaling pathways, supporting its potential as a therapeutic candidate for PC.
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10. Computational prioritization of megalin-aminoglycoside recognition and gentamicin-associated cellular stress responses.
PMID:日期:2026-09-19Aminoglycosides are effective antibiotics for severe infections, but their clinical use is limited by nephrotoxicity and ototoxicity resulting from drug accumulation in non-infected tissues. Megalin, an endocytic receptor expressed in renal proximal tubules and inner-ear tissues, has been proposed as a mediator of this uptake. To evaluate whether the CR10 domain of human megalin constitutes a plausible aminoglycoside-recognition site and to prioritize compounds for experimental testing. Seven aminoglycosides were comparatively analyzed in silico using docking and molecular dynamics simulations against megalin CR10. Gentamicin, which showed one of the most favorable predicted interaction profiles, was selected for biological evaluation. Cell viability was assessed in HEK293, HeLa, and U87MG cells, while calcium signaling and NF-κB activation were measured in HEK293 cells as indicators of cellular stress. Gentamicin reduced viability in a cell-type-dependent manner and induced calcium and NF-κB responses in HEK293 cells. Computational analyses suggested predominantly electrostatic interactions with megalin CR10, with gentamicin, tobramycin, and neomycin showing the most favorable predicted binding energies. The experimental and computational findings support a sequential in silico-to-in vitro workflow in which cellular assays define a gentamicin-associated stress phenotype, while molecular modeling identifies megalin CR10 as a structurally plausible aminoglycoside-recognition region that may contribute to tissue uptake or retention in organs expressing LRP2/megalin.