Journal of Biological Inorganic Chemistry最新文献_第3页

Catecholase activity, DNA cleavage and cytotoxicity of six Zn(II) complexes synthesized from designed Mannich ligands: higher reactivity of mononuclear over dinuclear 由设计的曼尼希配体合成的6种锌（II）配合物的儿茶酚酶活性、DNA切割和细胞毒性：单核比双核的反应性更高。

IF 2.8 3区化学

Journal of Biological Inorganic Chemistry Pub Date : 2026-07-14 DOI: 10.1007/s00775-026-02156-x

Ria Sanyal, Sandeep Kumar Dash, Sudhanshu Das, Sourav Chattopadhyay, Somenath Roy, Debasis Das

引用次数: 0

Iron–ascorbate complex formation and redox behavior in Tris buffer under aerobic and anaerobic conditions: relevance to iron-deficiency anemia 好氧和厌氧条件下Tris缓冲液中铁-抗坏血酸复合物的形成和氧化还原行为：与缺铁性贫血的相关性

IF 2.8 3区化学

Journal of Biological Inorganic Chemistry Pub Date : 2026-07-04 DOI: 10.1007/s00775-026-02162-z

Manmeet Singh, Jayanta Bag, Manas Khatua, Biplab K Maiti

{"title":"Iron–ascorbate complex formation and redox behavior in Tris buffer under aerobic and anaerobic conditions: relevance to iron-deficiency anemia","authors":"Manmeet Singh, Jayanta Bag, Manas Khatua, Biplab K Maiti","doi":"10.1007/s00775-026-02162-z","DOIUrl":"10.1007/s00775-026-02162-z","url":null,"abstract":"<div><p>Iron–ascorbate (Fe–Asc) is a clinically approved drug for iron-deficiency anemia (IDA), yet its formation and redox behavior under varying conditions remain poorly understood. Herein, we report the first comprehensive examination of Fe–Asc formation and redox reactivity in Tris buffer as a function of stoichiometry, pH, and oxygen availability. Oxidation of Fe(II) in air-saturated buffer accelerates with pH, yielding multiple species, primarily di- and tri-nuclear clusters. Notably, FeSO₄ with AscH produces a distinct purple complex (λ<sub>max</sub> = 510 nm), whose assembly depends critically on O₂, 1:3 stoichiometry of Fe: AscH, and buffer pH 7.5, whereas no such species forms anaerobically. ESI-MS suggests trinuclear clusters, whose stability and redox dynamics are monitored by time-resolved absorbance. The purple color disappears with dithionite or H₂O₂, but dithionite-treated samples regain color upon air exposure, demonstrating redox reversibility. Electrochemically, FeSO₄ shows cathodic (-0.32 V) and anodic (-0.06 V) peaks vs. Ag/AgCl, but the cathodic current decreases markedly in presence of AscH, reflecting Fe–Asc interactions. EPR spectra of FeSO₄ and FeSO₄/AscH are similar, with g = 9.43, 4.37 (high-spin Fe(III), S = 5/2) and g = 1.92 (S = ½, [Fe(III)–Fe(II)] coupling). These results suggest the formation of mixed valence trinuclear clusters with a dynamic ligand environment.</p><h3>Graphical Abstract</h3><p>The interaction between Fe and AscH with a specific stoichiometric ratio (Fe: AscH; 1:3), in Tris-buffer at pH7.5 under aerobic conditions, forms a purple complex, suggested as a mixed valence cluster, whereas anaerobic or dithionite-treated purple solutions yield a colorless solution that can reversibly interconvert with the purple form.</p><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 5","pages":"421 - 444"},"PeriodicalIF":2.8,"publicationDate":"2026-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148387205","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}

引用次数: 0

The development of bioinspired copper complexes for CO2 activation and hydration 用于CO2活化和水化的仿生铜配合物的研制。

IF 2.8 3区化学

Journal of Biological Inorganic Chemistry Pub Date : 2026-06-22 DOI: 10.1007/s00775-026-02155-y

Ramamoorthy Ramasubramanian, Jyun-Chi Lee, Rui-Ze Xu, Xylon Weng, Tiow-Gan Ong, Sodio C. N. Hsu, Glenn P. A. Yap, Vincent C.-C. Wang

{"title":"The development of bioinspired copper complexes for CO2 activation and hydration","authors":"Ramamoorthy Ramasubramanian, Jyun-Chi Lee, Rui-Ze Xu, Xylon Weng, Tiow-Gan Ong, Sodio C. N. Hsu, Glenn P. A. Yap, Vincent C.-C. Wang","doi":"10.1007/s00775-026-02155-y","DOIUrl":"10.1007/s00775-026-02155-y","url":null,"abstract":"<div><p>Here, we report a thioether-modified pyridine-2,6-dicarboxamide copper complex, [Cu(L)], <b>1</b> and its hydroxide-bridged dimer form, <b>2</b> exhibit different mechanisms of CO<sub>2</sub> activation. The incorporation of a thioether moiety enhances the stabilization of the Cu(I) state and improves the redox reversibility of the complex for CO<sub>2</sub> activation. While <b>1</b> monomer shows no direct reactivity toward CO<sub>2</sub> in its resting state, the µ-OH dimer <b>2</b> reacts with CO<sub>2</sub> to form a bicarbonate species, mimicking the nucleophilic CO<sub>2</sub> hydration observed in Zn-containing carbonic anhydrases. In comparison, upon reduction, <b>1</b> forms a CO<sub>2</sub>-bound intermediate, revealing a redox-triggered pathway distinct from that of <b>2</b>. Under electrochemical conditions, both complexes exhibit irreversible Cu(II/I) reduction in the presence of CO<sub>2</sub>, wherein an initial electron-transfer (E) step is followed by a chemical (C) transformation involving transient Cu-CO<sub>2</sub> (EC-type) adduct formation. Overall, these findings demonstrate that the incorporation of soft sulfur donors equips copper complexes to mediate CO<sub>2</sub> reactivity, providing a new direction toward the design of copper-based catalysts for CO<sub>2</sub> conversion. </p></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 5","pages":"351 - 357"},"PeriodicalIF":2.8,"publicationDate":"2026-06-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148292901","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}

引用次数: 0

Retraction Note: Surface modification minimizes the toxicity of silver nanoparticles: an in vitro and in vivo study 撤回注：表面改性最大限度地减少银纳米颗粒的毒性：一项体外和体内研究。

IF 2.8 3区化学

Journal of Biological Inorganic Chemistry Pub Date : 2026-06-15 DOI: 10.1007/s00775-026-02157-w

Balaram Das, Satyajit Tripathy, Jaydeep Adhikary, Sourav Chattopadhyay, Debasis Mandal, Sandeep Kumar Dash, Sabyasachi Das, Aditi Dey, Sankar Kumar Dey, Debasis Das, Somenath Roy

引用次数: 0

A meeting of minds, mechanisms and memories – editorial to JBIC Special Issue on Bio-electrochemistry in honor of Fraser Armstrong 思想、机制和记忆的相遇——为纪念弗雷泽·阿姆斯特朗，JBIC生物电化学特刊社论。

IF 2.8 3区化学

Journal of Biological Inorganic Chemistry Pub Date : 2026-06-06 DOI: 10.1007/s00775-026-02154-z

Rhiannon Evans, Clare Megarity, Alison Parkin

引用次数: 0

Correction: The evolutionary footprint of histidine in hemoglobin and myoglobin: an implication towards their function 更正：组氨酸在血红蛋白和肌红蛋白中的进化足迹：对其功能的暗示。

IF 2.8 3区化学

Journal of Biological Inorganic Chemistry Pub Date : 2026-05-28 DOI: 10.1007/s00775-026-02152-1

Jayraj Biswas, Kauseki Dutta, Kakali Biswas, Raja Banerjee

引用次数: 0

Pharmacokinetics and Efficacy of a Cyanide-Neutralizing [Mo2O2(µ-S)2]2+ Based Metallodrug in NMRI Mice 一种氰化物中和[Mo2O2（µ-S）2]2+型金属药物在NMRI小鼠体内的药代动力学及疗效

IF 2.8 3区化学

Journal of Biological Inorganic Chemistry Pub Date : 2026-05-25 DOI: 10.1007/s00775-026-02153-0

Linda A. Hancock, Bergthora Eiriksdottir, Sigridur G. Suman

{"title":"Pharmacokinetics and Efficacy of a Cyanide-Neutralizing [Mo2O2(µ-S)2]2+ Based Metallodrug in NMRI Mice","authors":"Linda A. Hancock, Bergthora Eiriksdottir, Sigridur G. Suman","doi":"10.1007/s00775-026-02153-0","DOIUrl":"10.1007/s00775-026-02153-0","url":null,"abstract":"<div><p>Hydrogen cyanide gas formation and subsequent contribution to inhalation injuries caused by residential and industrial fires is an increasing concern in public health care. Currently used cyanide antidotes are limited in their routes of administration and mechanisms of action. A potential cyanide antidote based on the [Mo<sub>2</sub>O<sub>2</sub>(μ-S)<sub>2</sub>]<sup>2</sup>+ core was assessed for its pharmacokinetic behavior and its efficacy in combating acute cyanide poisoning by inhalation in a mouse model. Pharmacokinetic studies revealed rapid absorption of the molybdenum compound into the bloodstream after intraperitoneal injection, and its complete elimination within eight hours. Prophylactic and therapeutic treatments with the compound by itself, and as a catalytic drug co-administered with thiosulfate, resulted in increased survival at lethal hydrocyanic acid concentrations.</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":"31 6","pages":"489 - 505"},"PeriodicalIF":2.8,"publicationDate":"2026-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-026-02153-0.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148013016","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}

引用次数: 0

The first and second zinc finger domains from Poly-ADP-ribose polymerase 1 (PARP1) are modified by hydrogen sulfide 聚adp核糖聚合酶1 （PARP1）的第一和第二锌指结构域被硫化氢修饰。

IF 2.8 3区化学

Journal of Biological Inorganic Chemistry Pub Date : 2026-05-22 DOI: 10.1007/s00775-026-02134-3

Ayanna J. Williams, Sarah L. J. Michel

{"title":"The first and second zinc finger domains from Poly-ADP-ribose polymerase 1 (PARP1) are modified by hydrogen sulfide","authors":"Ayanna J. Williams, Sarah L. J. Michel","doi":"10.1007/s00775-026-02134-3","DOIUrl":"10.1007/s00775-026-02134-3","url":null,"abstract":"<div><p>Poly(ADP-ribose) polymerase 1 (PARP1) is a Zinc Finger (ZF) protein that is involved in DNA damage response. PARP1 contains three zinc finger (ZF) domains, two with a Cys<sub>2</sub>HisCys (CCHC) ligand set and one with a Cys<sub>4</sub> (CCCC) ligand set that coordinate zinc. Persulfidation of cysteine residues in proteins is a new type of post-translational modification (PTM), for which ZFs are emerging as frequently modified. PARP1 has been identified as persulfidated in several cellular based persulfide-specific proteomics studies across several different cell types. Here, we examine PARP1 persulfidation by H<sub>2</sub>S. Two PARP1 peptide constructs, shPARP1-ZF1 and shPARP1-ZF2, were synthesized, purified, and shown to bind zinc and fold, using Co(II)/Zn(II) UV-visible (UV) monitored titrations and circular dichroism (CD) spectroscopy. The reactivity of the PARP ZFs with H<sub>2</sub>S was assessed using a UV-visible monitored 4-chloro-7-nitrobenzofurazan (NBF-Cl)/dimedone switch-tagging approach. Persulfidation for both PARP1 peptide constructs was observed under zinc-bound, oxygenated conditions. Superoxide intermediates were detected during the reaction using both dihydroethidine fluorescence and superoxide dismutase trapping. Together, these findings provide evidence that CCHC-type PARP ZFs can undergo persulfidation when Zn is bound and provide support for persulfidation being a general post-translational (PTM) modification for ZFs with different secondary structural elements.</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":"31 4","pages":"279 - 291"},"PeriodicalIF":2.8,"publicationDate":"2026-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13215146/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148004202","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}

引用次数: 0

Impact of the spatial distribution of positive charges on the catalytic activity of NiSOD bioinspired complexes 正电荷空间分布对NiSOD生物激发复合物催化活性的影响。

IF 2.8 3区化学

Journal of Biological Inorganic Chemistry Pub Date : 2026-05-19 DOI: 10.1007/s00775-026-02150-3

Pawel Guinard, Jacques Pécaut, Alan Le-Goff, Carole Duboc, Pascale Delangle, Sarah Hostachy

{"title":"Impact of the spatial distribution of positive charges on the catalytic activity of NiSOD bioinspired complexes","authors":"Pawel Guinard, Jacques Pécaut, Alan Le-Goff, Carole Duboc, Pascale Delangle, Sarah Hostachy","doi":"10.1007/s00775-026-02150-3","DOIUrl":"10.1007/s00775-026-02150-3","url":null,"abstract":"<div><p>In order to mitigate superoxide-induced damage, cells rely on superoxide dismutases (SODs), a family of metalloenzymes that catalyze the dismutation of superoxide. These enzymes display a positively-charged substrate entrance channel for superoxide guidance to the active metal center. ATCUN-like Ni(II) complexes have been shown to mimic NiSOD effectively and benefit from versatile peptide structures, which are ideal for introducing positive charges through arginine residues at various positions to modulate catalytic properties. We describe here five novel ATCUN-like Ni(II) complexes, with arginines at various positions in close proximity to the metal center. All the peptides form monometallic square planar Ni(II) complexes in water at pH 7.4, with either a N<sub>2</sub>S<sub>2</sub> coordination (<i>S</i>-series) or an equilibrium between N<sub>2</sub>S<sub>2</sub> and N<sub>3</sub>S<sub>1</sub> coordination modes (<i>N/S</i>-series). The <i>S</i>-series demonstrates a clear beneficial effect of the charge increase from − 2 to + 2 on the pseudo-first order catalytic constant. Furthermore, the data obtained for the <i>N/S</i> complexes demonstrate that introducing an arginine residue in the central position of the ATCUN-like motif does not enhance activity, but actually impedes catalysis. These findings show that both the distance of the charged residues from the metal center and their positioning in space are of prime importance.</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":"31 4","pages":"303 - 312"},"PeriodicalIF":2.8,"publicationDate":"2026-05-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-026-02150-3.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147969440","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}

引用次数: 0

Crystallise, poise, capture: a multimodal platform for correlated structural and spectroscopic characterisation of redox enzymes 结晶，平衡，捕获：氧化还原酶的相关结构和光谱表征的多模态平台。

IF 2.8 3区化学

Journal of Biological Inorganic Chemistry Pub Date : 2026-05-05 DOI: 10.1007/s00775-026-02148-x

Shoba Laxmi, Sofia Jaho, William K. Myers, Kylie A. Vincent, Stephen B. Carr

{"title":"Crystallise, poise, capture: a multimodal platform for correlated structural and spectroscopic characterisation of redox enzymes","authors":"Shoba Laxmi, Sofia Jaho, William K. Myers, Kylie A. Vincent, Stephen B. Carr","doi":"10.1007/s00775-026-02148-x","DOIUrl":"10.1007/s00775-026-02148-x","url":null,"abstract":"<div><p>Iron–sulfur (Fe-S) clusters are ubiquitous as redox-active protein cofactors, but it is often difficult to collect protein structures in which redox centres are in uniform and well-defined oxidation states. Using spinach ferredoxin I (Fdx) as a model redox protein, we demonstrate an integrated methodological pathway for electrochemical modulation of redox state in protein crystals coupled with in crystallo EPR and online-UV-visible spectroscopy to verify oxidation state. We show that Fdx crystals can be electrochemically reduced, reversibly, without compromising lattice integrity or X-ray diffraction quality. We show that redox levels can be precisely ascertained in crystallo via EPR and UV-visible spectroscopy, enabling a direct correlation between protein structure and electronic state of the metal cluster. In this way, we generate and compare ’oxidised’, ‘reduced’ and ‘re-oxidised’ structures of Fdx. Overall, our approach demonstrates a pipeline which will be applicable to structure-function studies of a wide range of electron-transfer proteins and redox enzymes.</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":"31 on","pages":"153 - 162"},"PeriodicalIF":2.8,"publicationDate":"2026-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-026-02148-x.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147832006","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}

引用次数: 0