Journal of Inorganic Biochemistry最新文献

{"title":"Corrigendum to \"New insights into the O₂-sensing mechanism of FixL and other gas sensing heme proteins\" [Journal of Inorganic Biochemistry 259 (2024) 112642].","authors":"Mark F Reynolds","doi":"10.1016/j.jinorgbio.2024.112746","DOIUrl":"10.1016/j.jinorgbio.2024.112746","url":null,"abstract":"","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":" ","pages":"112746"},"PeriodicalIF":3.8,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142338548","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to \"Monomeric copper(II) complexes with unsymmetrical salen environment: Synthesis, characterization and study of biological activities\" [Journal of Inorganic Biochemistry 253 (2024) 112497].","authors":"Deepika Mohapatra, Sushree Aradhana Patra, Pratikshya Das Pattanayak, Gurunath Sahu, Takashi Nakamura, Takahiro Sasamori, Rupam Dinda","doi":"10.1016/j.jinorgbio.2024.112753","DOIUrl":"10.1016/j.jinorgbio.2024.112753","url":null,"abstract":"","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":" ","pages":"112753"},"PeriodicalIF":3.8,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142378937","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Quantification of lysosomal labile Zn²⁺ and monitoring of Zn²⁺ efflux using a small-molecule-protein hybrid fluorescent probe.","authors":"Yuyin Du, Toshiyuki Kowada, EunHye Sung, Rong Liu, Andrei Soloviev, Toshitaka Matsui, Shin Mizukami","doi":"10.1016/j.jinorgbio.2024.112811","DOIUrl":"https://doi.org/10.1016/j.jinorgbio.2024.112811","url":null,"abstract":"<p><p>Lysosomal labile Zn²⁺ levels have been unclear. By targeting a small-molecule fluorescent Zn²⁺ probe, ZnDA-3H, to lysosomes via VAMP7-Halo, the lysosomal labile Zn²⁺ concentration was determined to be 1.9 nM in HeLa cells. Furthermore, ZnDA-3H enabled direct visualization of the Zn²⁺ efflux from the lysosomes to cytosol upon TRPMLs activation.</p>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"264 ","pages":"112811"},"PeriodicalIF":3.8,"publicationDate":"2024-12-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142823702","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Solution equilibrium and redox properties of metal complexes with 2-formylpyridine guanylhydrazone derivatives: Effect of morpholine and piperazine substitutions.","authors":"Gerda T Gátszegi, Tatsiana V Petrasheuskaya, Nóra V May, Bálint Hajdu, Gabriella Spengler, Felix Bacher, Sergiu Shova, Vladimir B Arion, Éva A Enyedy","doi":"10.1016/j.jinorgbio.2024.112812","DOIUrl":"https://doi.org/10.1016/j.jinorgbio.2024.112812","url":null,"abstract":"<p><p>Schiff bases derived from aminoguanidine are extensively investigated for their structural versatility. The tridentate 2-formylpyridine guanylhydrazones act as analogues of 2-formyl or 2-acetylpyridine thiosemicarbazones, where the thioamide unit is replaced by the guanidyl group. Six derivatives of 2-formylpyridine guanylhydrazone were synthesized and their proton dissociation and complex formation processes with Cu(II), Fe(II) and Fe(III) ions were studied using pH-potentiometry, UV-visible, NMR and electron paramagnetic resonance spectroscopic methods. The ligands have substituents such as amine, morpholine, N-methyl-piperazine at different positions of the pyridine ring. The influence of the different structural elements on the solution chemical properties and cytotoxicity has been disclosed. The solid state structure of four ligands was determined by X-ray crystallography. The ligands bind to Cu(II) in a tridentate fashion via an (N,N,N) donor set, forming mono-ligand complexes. However, for ligands with heterocyclic morpholine and piperazine nitrogen atoms in coordination position a tetradentate binding was observed. Despite the additional coordinating donor atom, the stability of these Cu(II) complexes showed little or no increase. The Cu(II), Fe(II) and Fe(III) complexes of the studied 2-formylpyridine guanylhydrazones exhibited significantly lower stability compared to their corresponding 2-formyl or 2-acetylpyridine thiosemicarbazone analogues. The ligands underwent slow partial hydrolysis (and oxidation) in the presence of Cu(II) ions, leading to the formation of new ligands through the reorganization of structural components around the metal ion. Additionally, the studied Cu(II) complexes demonstrated a great propensity for reduction by glutathione. All these features contributed to the finding that these 2-formylpyridine guanylhydrazones and their Cu(II) complexes did not display measurable cytotoxic activity.</p>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"264 ","pages":"112812"},"PeriodicalIF":3.8,"publicationDate":"2024-12-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142862847","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Reinvestigation of the mechanism of dioxygen activation at a Mn^II(cyclam) center.","authors":"Tarali Devi, Stefan Mebs, Dibya Jyoti Barman, Amanda Opis-Basilio, Michael Haumann, Kallol Ray","doi":"10.1016/j.jinorgbio.2024.112809","DOIUrl":"https://doi.org/10.1016/j.jinorgbio.2024.112809","url":null,"abstract":"<p><p>This study deals with the unprecedented reactivity of a [(cyclam)Mn^II(OTf)₂] (3-cis; OTf = CF₃SO_3^-) with O₂, which, depending on the presence or absence of a hydrogen atom donor like 1-hydroxy-2,2,6,6-tetramethyl-piperidine (TEMPO-H), selectively generates di-μ-oxo Mn(III)Mn(IV) (1) or Mn^IV₂ (2) complexes, respectively. Both dimers have been characterized by different techniques including single-crystal X-ray diffraction, X-ray absorption spectroscopy, and electron paramagnetic resonance. Oxygenation reactions carried out with labeled ¹⁸O₂ and Resonance Raman spectroscopy unambiguously show that the oxygen atoms present in the Mn^IVMn^III dimer originate from O₂. Experimental evidences are provided for a novel method of dioxygen activation involving three Mn ions or two Mn ions and TEMPO-H to generate the bis(μ-oxo)dimanganese(IV) or bis(μ-oxo) dimanganese(III, IV) cores, respectively.</p>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"264 ","pages":"112809"},"PeriodicalIF":3.8,"publicationDate":"2024-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142870912","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural insights into temperature-dependent dynamics of METPsc1, a miniaturized electron-transfer protein.","authors":"Luigi F Di Costanzo, Gianmattia Sgueglia, Carla Orlando, Maurizio Polentarutti, Linda Leone, Salvatore La Gatta, Maria De Fenza, Luca De Gioia, Angela Lombardi, Federica Arrigoni, Marco Chino","doi":"10.1016/j.jinorgbio.2024.112810","DOIUrl":"https://doi.org/10.1016/j.jinorgbio.2024.112810","url":null,"abstract":"<p><p>The design of protein-metal complexes is rapidly advancing, with applications spanning catalysis, sensing, and bioremediation. We report a comprehensive investigation of METPsc1, a Miniaturized Electron Transfer Protein, in complex with cadmium. This study elucidates the impact of metal coordination on protein folding and structural dynamics across temperatures from 100 K to 300 K. Our findings reveal that METPsc1, composed of two similar halves stabilized by intramolecular hydrogen bonds, exhibits a unique \"clothespin-like\" recoil mechanism. This allows it to adapt to metal ions of varying radii, mirroring the flexibility observed in natural rubredoxins. High-resolution crystallography and molecular dynamics simulations unveil concerted backbone motions and subtle temperature-dependent shifts in side-chain conformations, particularly for residues involved in crystal packing. Notably, CdS bond lengths increase with temperature, correlating with anisotropic motions of the sulfur atoms involved in second-shell hydrogen bonding. This suggests a dynamic role of protein matrix upon redox cycling. These insights into METPsc1 highlight its potential for catalysis and contribute to the designing of artificial metalloproteins with functional plasticity.</p>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"264 ","pages":"112810"},"PeriodicalIF":3.8,"publicationDate":"2024-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142845496","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Induction of ferroptosis of iridium(III) complexes localizing at the mitochondria and lysosome by photodynamic therapy.","authors":"Yajie Niu, Shuanghui Tang, Jiongbang Li, Chunxia Huang, Yan Yang, Lin Zhou, Yunjun Liu, Xiandong Zeng","doi":"10.1016/j.jinorgbio.2024.112808","DOIUrl":"https://doi.org/10.1016/j.jinorgbio.2024.112808","url":null,"abstract":"<p><p>In this study, [Ir(ppy)₂(DMHBT)](PF₆) (ppy = deprotonated 1-phenylpyridine, DMHBT = 10,12-dimethylpteridino[6,7-f][1,10]phenanthroline-11,13-(10,12H)-dione, 8a), [Ir(bzq)₂(DMHBT)](PF₆) (bzq = deprotonated benzo[h]quinoline, 8b) and [Ir(piq)₂(DMHBT)](PF₆) (piq = deprotonated 1-phenylisoquinoline, 8c) were synthesized and characterized by HRMS, ¹³C NMR and ¹H NMR. In vitro cytotoxicity experiments showed that 8a, 8b, 8c show moderate cytotoxicity against B16 cells, while the cytotoxicity of the complexes 8a, 8b and 8c toward B16 cells was greatly improved upon light irradiation, which can be used as photosensitizers to exert anticancer efficacy in photodynamic therapy (PDT). After being taken up by cells, 8a, 8b, 8c were localized in the mitochondria, resulting in a large amount of Ca²⁺ in-flux, a burst release of ROS, a sustained opening of mitochondrial permeability transition pore, and a decrease of the mitochondrial membrane potential, which led to mitochondrial dysfunction and further activation of caspase 3 and Bcl-2 family proteins to induce apoptosis. Overloaded ROS reacted with polyunsaturated fatty acids on the cell membrane, and initiated lipid peroxidation, inhibited the x_c^--system-glutathione (GSH)-glutathione peroxidase 4 (GPX4) antioxidant defense system, and upregulated the expression of the damage-associated molecules, HMGB1, CRT, and HSP70. The presence of Fer-1 was effective on increasing the cell survival, which demonstrates that the complexes possess the potential to induce ferroptosis and immunogenic cell death. In addition, 8a, 8b and 8c induced autophagy by inhibiting the AKT/PI3K/mTOR signaling pathway, downregulating p62 and promoting Beclin-1 expression upon light irradiation.</p>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"264 ","pages":"112808"},"PeriodicalIF":3.8,"publicationDate":"2024-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142821652","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antioxidant effect, DNA-binding, and transport of the flavonoid acacetin influenced by the presence of redox-active Cu(II) ion: Spectroscopic and in silico study.","authors":"Marek Štekláč, Michal Malček, Peter Gajdoš, Simona Vevericová, Milan Čertík, Marián Valko, Vlasta Brezová, Miriama Malček Šimunková","doi":"10.1016/j.jinorgbio.2024.112802","DOIUrl":"https://doi.org/10.1016/j.jinorgbio.2024.112802","url":null,"abstract":"<p><p>Acacetin (AC) is a natural polyphenol from the group of flavonoids. It is well established that the behavior of flavonoids depends on the presence of redox-active substances; therefore, we aim to investigate their biological activity following the interaction with Cu(II) ion. Our study demonstrates that AC can effectively bind Cu(II) ions, as confirmed by UV-Vis and EPR spectroscopy as well as DFT calculations. AC appears as a potent scavenger against the model ABTS radical cation by itself, but this ability is significantly limited upon Cu(II) coordination. The possible mild synergistic effect of AC in the presence of vitamin C and glutathione was also shown by the ABTS^•+ test. In contrast, an inhibitory effect was observed in the presence of Cu(II) ions. The equimolar addition of AC to the model Fenton-like system containing Cu(II) did not have a noticeable effect on the concentration of hydroxyl radicals produced, but in its excess the formation of ^•OH decreased, as proved by EPR spin trapping. Absorption titrations and gel electrophoresis revealed effective binding to calf thymus (CT)-DNA with a stronger interaction for the Cu(II)-AC complex. The detailed mode of binding to biomolecules was described using molecular docking and molecular dynamics. Obtained results indicate that the double helix of DNA unwinds after interaction with the Cu(II)-AC complex. Fluorescence spectroscopy, employing human serum albumin (HSA), suggested a potential transport capacity for both AC and its Cu(II) complex.</p>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"264 ","pages":"112802"},"PeriodicalIF":3.8,"publicationDate":"2024-12-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142821651","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Unraveling the mechanism: How does β-phosphoglucomutase from the haloacid dehalogenase superfamily catalyze the interconversion of β-d-glucose 1-phosphate and β-d-glucose 6-phosphate? A chemical perspective.","authors":"Hao Zhang, Mingming Zhang, Kangning Zhu, Yulan Feng, Ling Yang, Wanjian Ding","doi":"10.1016/j.jinorgbio.2024.112794","DOIUrl":"https://doi.org/10.1016/j.jinorgbio.2024.112794","url":null,"abstract":"<p><p>The catalytic mechanisms of enzymes can be phylogenetically mapped corresponding to their catalytic structures. This mapping effectively elucidates the diversity of enzyme catalytic mechanisms and the emergence of new enzymatic activities within enzyme superfamilies. The haloacid dehalogenase (HAD) superfamily serves as an exemplary model system for comprehending the co-evolution of catalytic structures and mechanisms. This study delves into the mechanism underlying the functional divergence of β-phosphoglucomutase (β-PGM) from the phosphatase branch of the HAD superfamily, employing a chemical perspective. Through the construction and calculation of three models of varying scales using the Density Functional Theory method with B3LYP function, we aim to investigate the chemical mechanism driving this functional divergence of β-PGM from the HAD family. The computational results indicate that residues His20 and Lys76 in the second shell stabilize substrates and enhance the acid-base catalytic ability of Asp10. Additionally, residues Arg49, Ser116 and Asn118 facilitate substrate binding by engaging in close hydrogen bonding interactions with the substrates. Through cooperative action, these residues enable β-PGM to function as an efficient phosphoglucomutase. Through computational modeling and a chemical perspective, we unravel the mechanisms enabling β-PGM to convert β-d-glucose 1-phosphate to β-d-glucose 6-phosphate. Finally, based on the analysis of the evolutionary tree, we discussed and summarized the evolutionary relationships among different forms of metal cores of hydrolases.</p>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"264 ","pages":"112794"},"PeriodicalIF":3.8,"publicationDate":"2024-12-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142816954","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Insight into uranyl binding by cyclic peptides from molecular dynamics and density functional theory.","authors":"James A Platts, Iogann Tolbatov","doi":"10.1016/j.jinorgbio.2024.112793","DOIUrl":"https://doi.org/10.1016/j.jinorgbio.2024.112793","url":null,"abstract":"<p><p>It is a challenging task to develop uranyl-chelating agents based on peptide chemistry. A recently developed cationic dummy atom model of uranyl in conjunction with the classical molecular dynamics simulation presents a helpful utility to study the chelation of uranyl by peptides with a low computational cost. In the present study, it was used to describe the chelation of uranyl by the cyclic decapeptide with 4 Glu residues cyc-GluArgGluProGlyGluTrpGluProGly and its derivatives containing two phosphorylated serines in place of two Glu, termed pS16, pS18, pS38, and pS68. The obtained structures were further studied by density functional theory (DFT) and subsequent density analysis. We show that a combination of steered molecular dynamics and simulated annealing, using standard forcefields for peptide with the cationic dummy atom model of uranyl, can quickly and reliably obtain binding modes of uranyl-peptide complexes. Classical molecular dynamics simulation in explicit water produces geometry very close to the DFT-optimized structure. The presence of uranyl completely changes the conformation of these cyclic peptides from unstructured to organised. The simulation of a peptide with two uranyl units explained why only the 1:1 ratio of peptide and chelated-uranyl is observed experimentally in most cases, by the insufficiency of the anionic residues for the chelation of two UO₂²⁺ units, but that pS16 can accommodate two such units.</p>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"264 ","pages":"112793"},"PeriodicalIF":3.8,"publicationDate":"2024-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142790833","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}