Journal of Inorganic Biochemistry最新文献

{"title":"Pyridine alcohols: New applications reviving interest in metal complexes of a classical ligand","authors":"Magdalena Malik ,&nbsp;Tomasz Mazur ,&nbsp;Debbie C. Crans ,&nbsp;Urszula K. Komarnicka","doi":"10.1016/j.jinorgbio.2025.112880","DOIUrl":"10.1016/j.jinorgbio.2025.112880","url":null,"abstract":"<div><div>Pyridine-based alcohols and their metal complexes show unique characteristics, such as redox activity, variable coordination modes, and reactivity towards organic substrates, resulting in multifaceted properties and diverse applications. This review explores the structural properties of these ligands when coordinated to metal ions, particularly focusing on their ability to form mononuclear and polynuclear complexes with transition metals such as copper, manganese, nickel, and cobalt. Moreover, square planar complexes with silver, platinum, palladium, and gold are discussed as well. Structural studies have revealed various coordination geometries of these complexes, providing insights into their potential applications in various fields. We focus mainly on recent literature (2014–2024) and describe the structural and biological effects of the complexes. Despite the seeming obscurity of pyridine alcohol derivative ligands, we wish to emphasize their potential and the significant applications reported, highlighting the renewed interest in synthesizing coordination complexes with various metal ions.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"269 ","pages":"Article 112880"},"PeriodicalIF":3.8,"publicationDate":"2025-03-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143611080","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":"Identification of Ni2+-binding peptides in sunflower meal protein hydrolysate for deeper understanding of peptide-metal interactions","authors":"Jairo Andrés Camaño Echavarría ,&nbsp;Christelle Mathé ,&nbsp;Jean-Michel Girardet ,&nbsp;Cédric Paris ,&nbsp;Chibuike C. Udenigwe ,&nbsp;Katalin Selmeczi ,&nbsp;Laetitia Canabady-Rochelle","doi":"10.1016/j.jinorgbio.2025.112877","DOIUrl":"10.1016/j.jinorgbio.2025.112877","url":null,"abstract":"<div><div>Sunflower (<em>Helianthus annus</em> L.) is one of the most important oil crops in the world. Once oil extracted, sunflower meal by-product could offer a potential alternative for various food applications due to its high protein content. Derived from food protein hydrolysates, metal-binding peptides have attracted attention as bioactive compounds to prevent metal-induced oxidation and diseases. This study aimed to investigate the Ni²⁺-binding ability of sunflower meal protein hydrolysates and ten peptides theoretically present in sunflower proteins using IMAC, switchSENSE®, UV–vis and CD techniques. Single and sequential enzymatic treatments were applied to produce hydrolysates using Protamex® (Prot) and Protamex followed by Flavourzyme® (Prot+Flav), respectively. MS/MS analysis of enriched Ni²⁺-binding peptides fractions revealed different composition of His-containing peptides among hydrolysates; however, similar to the His-containing pure peptides, the Ni²⁺-binding ability of all the hydrolysates was almost identical in IMAC. On the contrary, switchSENSE® studies indicated that the Ni²⁺-binding ability of sunflower peptides does not depend only on the presence of His residues, but also on their position along the polypeptide chain and the presence of proline, suggesting that Prot hydrolysates exhibited the highest Ni²⁺-binding ability. UV–vis and CD data confirmed that sunflower peptides bound onto Ni²⁺ through nitrogen atoms from imidazole sidechain of His residues, deprotonated amide bonds and N-terminal amino group, indicating square-planar and also octahedral geometries in the formed complexes. Finally, His-containing peptides without proline could offer a suitable strategy to design metal-binding peptides from sunflower meal by-product, with the most promising motifs being LL<strong>H</strong>VT and WL<strong>H.</strong></div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"269 ","pages":"Article 112877"},"PeriodicalIF":3.8,"publicationDate":"2025-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143637330","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"An efficient circularly polarized luminescence probe base on anthryl-modified Eu(III)-helicates for the detection and imaging singlet oxygen in living cells","authors":"Xiumei Zhang ,&nbsp;Xinglu Wang ,&nbsp;Wenru Huang ,&nbsp;Sen Yin ,&nbsp;Pengfei Yan ,&nbsp;Ting Gao ,&nbsp;Yanyan Zhou ,&nbsp;Hongfeng Li","doi":"10.1016/j.jinorgbio.2025.112881","DOIUrl":"10.1016/j.jinorgbio.2025.112881","url":null,"abstract":"<div><div>Singlet oxygen (¹O₂) is the main active ingredient in photodynamic therapy (PDT). However, an excess ¹O₂ can cause unnecessary toxicity. Therefore, it is of great importance to develop reliable and sensitive methods or probes for detecting ¹O₂ in biological systems. In this study, a pair of anthryl-modified Eu(III) binaphthol-bis-β-diketones helicates, (NEt₄)₂[Eu₂(<strong>L</strong>^{<strong>R/S</strong>})₄] are designed, synthesized and characterized. Initially, the complexes display faint luminescence. Upon reacting with ¹O₂ to create endoperoxides of the anthracene framework, the long-lived luminescence of the Eu(III) complexes is activated. Notably, the high luminescence dissymmetry factor, g_lum of the ⁵D₀ → ⁷F₁ transition (595 nm) shows an obvious increase from −1.21 to −1.29 before and after oxidation. The complex exhibits a highly selective luminescent response to the ¹O₂ generated by 5-aminolevulinic acid (ALA) loaded 4 T1 cells during photodynamic processes. To the best of we knowledge, this is the first example of ¹O₂ detection based on circularly polarized luminescence (CPL) probe. The design of the lanthanide CPL probe provides a practical way for the sensitive detection of ¹O₂ in the future.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"269 ","pages":"Article 112881"},"PeriodicalIF":3.8,"publicationDate":"2025-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143591852","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":"Special issue on ‘Artificial metalloenzymes’","authors":"Anne-K. Duhme-Klair ,&nbsp;Nobutaka Fujieda","doi":"10.1016/j.jinorgbio.2025.112876","DOIUrl":"10.1016/j.jinorgbio.2025.112876","url":null,"abstract":"","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"267 ","pages":"Article 112876"},"PeriodicalIF":3.8,"publicationDate":"2025-03-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143584117","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":"Gaseous ligand binding to Porphyromonas gingivalis HmuY hemophore-like protein in complex with heme","authors":"Cécile Exertier ,&nbsp;Linda Celeste Montemiglio ,&nbsp;Lorenzo Tognaccini ,&nbsp;Carlotta Zamparelli ,&nbsp;Beatrice Vallone ,&nbsp;Teresa Olczak ,&nbsp;Michał Śmiga ,&nbsp;Giulietta Smulevich ,&nbsp;Francesco Malatesta","doi":"10.1016/j.jinorgbio.2025.112879","DOIUrl":"10.1016/j.jinorgbio.2025.112879","url":null,"abstract":"<div><div><em>Porphyromonas gingivalis</em> is the main pathogenic player in the development of periodontitis. To acquire heme, being an essential source of iron and protoporphyrin IX, <em>P. gingivalis</em> utilizes TonB-dependent outer membrane heme receptor (HmuR) and heme-binding hemophore-like protein (HmuY) as the main system for heme uptake from host hemoproteins. In this work, we present an extensive spectroscopic characterization of the binding of exogenous gaseous ligands to the holo-form of the HmuY (HmuY-heme) to unravel the mechanistic basis of heme release. Our data are consistent with a scenario where heme release from HmuY-heme is a multistep process that requires the initial rupture of one of the two heme‑iron coordination bonds with endogenous histidines.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"269 ","pages":"Article 112879"},"PeriodicalIF":3.8,"publicationDate":"2025-03-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143591853","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Resveratrol derivative modified Ru(II) complexes: Synthesis, characterization, in vitro and in vivo anticancer study","authors":"Wuyang Hua ,&nbsp;Fenglin Li ,&nbsp;Ping Yang ,&nbsp;Zhongkui Lu ,&nbsp;Yanxia Liu ,&nbsp;Bao Zhong ,&nbsp;Baoxing Shen","doi":"10.1016/j.jinorgbio.2025.112873","DOIUrl":"10.1016/j.jinorgbio.2025.112873","url":null,"abstract":"<div><div>The diversification of ligands provides more opportunities to adjust the photophysical performance as well as the bio-function of Ru(II) complexes as novel photosensitizers. Herein, a kind of Ru(II) complexes carrying resveratrol derivative, amino-Res, as ligand was designed and synthesized. The representative complex (named <strong>Ru4</strong>) showed potent anticancer activity under the trigger of 520 nm-light. Lipophilicity and cellular accumulation experiments indicated that <strong>Ru4</strong> possessed higher Log<em>P</em>_O/W value and cell up-take than <strong>Ru1</strong>-<strong>Ru3</strong> and [Ru(bpy)₃]²⁺. Mechanism study revealed that <strong>Ru4</strong> could inhibit cancer cell migration, invasion and cancer stemness. The bio-function of <strong>Ru4</strong> was mainly inherited from the amino-Res ligand. The <em>in vivo</em> study demonstrated that <strong>Ru4</strong> could inhibit the tumor growth without significant system toxicity.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"267 ","pages":"Article 112873"},"PeriodicalIF":3.8,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143551097","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":"Mechanistic insights into Staphylococcus aureus IsdG-Ferrochelatase interactions: A key to understanding haem homeostasis in pathogens","authors":"Mafalda R. Almeida ,&nbsp;Marco A.M. Videira ,&nbsp;João C. Lima ,&nbsp;Lígia Saraiva","doi":"10.1016/j.jinorgbio.2025.112878","DOIUrl":"10.1016/j.jinorgbio.2025.112878","url":null,"abstract":"<div><div>In this study, we explore the molecular interactions between two <em>Staphylococcus aureus</em> enzymes, the haem oxygenase IsdG and ferrochelatase CpfC. Based on our previous research showing that IsdG interacts specifically with ferrochelatase, we constructed several mutants of IsdG and determined by fluorescence anisotropy the kinetic and affinity parameters of the interaction between CpfC and IsdG mutants. Our data indicate that the interacting residues on CpfC are located on a surface region distant from the porphyrin binding pocket. The identified interactions suggest that the inhibition of CpfC's iron-coproporphyrin chelatase activity by IsdG arises from long-range interactions, rather than direct blocking of the active site. Altogether, the experimental data allowed defining the regions involved in the interaction between the two proteins. These findings illuminate the interplay between haem acquisition and biosynthesis in pathogens, emphasizing the importance of specific protein interactions in mitigating intracellular haem toxicity. By elucidating these molecular mechanisms, we advance our understanding of bacterial haem homeostasis and contribute to development of potential therapeutic targets for combating haem-dependent pathogenesis.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"269 ","pages":"Article 112878"},"PeriodicalIF":3.8,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143561857","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fluorescent half-salen phenoxy-imine zinc complexes to reveal exogenous and endogenous H2S","authors":"Alessio Trerotola ,&nbsp;Giuseppe Gravina ,&nbsp;Viktoriia Vykhovanets ,&nbsp;Naym Blal ,&nbsp;Daniela Guarnieri ,&nbsp;Andrea Maranzana ,&nbsp;Marina Lamberti ,&nbsp;Mina Mazzeo ,&nbsp;Maria Strianese","doi":"10.1016/j.jinorgbio.2025.112875","DOIUrl":"10.1016/j.jinorgbio.2025.112875","url":null,"abstract":"<div><div>In this contribution, the synthesis and the reactivity with HS⁻ of a family of half-salen Zn complexes are reported. We provide evidence that HS⁻ binds the zinc center of all the complexes under investigation. DFT and CCSD(T) calculations were performed to model the reactivity of these complexes with HS⁻.</div><div>We successfully applied a homoleptic zinc complex bearing a Schiff-based ligand with pyridine pendant arms as a probe for the monitoring of exogenous and endogenous H₂S levels in live cells.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"267 ","pages":"Article 112875"},"PeriodicalIF":3.8,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143551245","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Probing the generation, reactivity, and kinetics of high-valent manganese-oxo phthalocyanines: Insights into oxidation mechanisms","authors":"Alexis Smith,&nbsp;Sobenna Onyeso,&nbsp;Tristan Skipworth,&nbsp;Candice Schlabach,&nbsp;Rui Zhang","doi":"10.1016/j.jinorgbio.2025.112872","DOIUrl":"10.1016/j.jinorgbio.2025.112872","url":null,"abstract":"<div><div>In this study, manganese(IV)-oxo phthalocyanines [Mn^IV(Pc)(O)] (<strong>3</strong>) (Pc = phthalocyanine) were produced either through visible light photolysis of [Mn^III(Pc)(ClO₃)] or by chemical oxidation of [Mn^III(Pc)Cl] (<strong>1</strong>) with iodobenzene diacetate. The manganese(IV)-oxo species under study include tetra-<em>tert</em>-butylphthalocyaine‑manganese(IV)-oxo (<strong>3a</strong>) and phthalocyanine‑manganese(IV)-oxo (<strong>3b</strong>). As anticipated, the generated <strong>3</strong> reacted with various organic substrates to yield the oxidized products and further proved to be a competent oxidant via an H₂¹⁸O isotope labeling experiment. The kinetics of oxygen atom transfer (OAT) reactions for these generated <strong>3</strong> species with a range of substrates were examined in CH₃CN solutions unless other specified. Overall, the second-order rate constants under pseudo-first-order conditions for <strong>3a</strong> and <strong>3b</strong> with the same substrates display similar modest reactivity, with the nature of the substrate playing a major role in influencing the reactivity of species <strong>3</strong>. The phenol substrates, in particular, reacted the fastest. Of note, second-order rate constants determined for thioanisoles are comparable to those of alkene epoxidations and activated C<img>H bond oxidations. Conventional Hammett analyses of rate constants for substituted styrenes revealed a linear correlation with the σ constant, indicating minimal charge developed at the transition state during the oxidation process. Additionally, the competition product studies and the Hammett correlation analysis further suggested that the manganese(IV)-oxo species observed in those kinetic studies are unlikely to serve as the primary oxidant for the epoxidation reactions catalyzed by manganese(III) phthalocyanine with PhI(OAc)₂.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"267 ","pages":"Article 112872"},"PeriodicalIF":3.8,"publicationDate":"2025-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143551246","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":"Heme dependent activity of the Streptomyces c-di-GMP-metabolizing enzyme CdgA","authors":"Olaf Latta ,&nbsp;Emily E. Weinert ,&nbsp;Andreas Bechthold","doi":"10.1016/j.jinorgbio.2025.112874","DOIUrl":"10.1016/j.jinorgbio.2025.112874","url":null,"abstract":"<div><div><em>Streptomyces</em> species are vital for producing natural products like antibiotics, with <em>c</em>-di-GMP playing a key role in regulating processes such as differentiation. <em>C</em>-di-GMP metabolism is controlled by diguanylate cyclases (DGCs) and phosphodiesterases (PDEs), which synthesize and hydrolyze <em>c</em>-di-GMP, respectively, to modulate cellular levels. To improve our understanding of <em>c</em>-di-GMP-regulated processes in <em>Streptomyces</em>, we have characterized a <em>c</em>-di-GMP-metabolizing enzyme CdgA from <em>Streptomyces ghanaensis</em> that contains both a diguanylate cyclase and a phosphodiesterase domain. Our studies demonstrate that the enzyme is purified in a form without heme and is only able to degrade <em>c</em>-di-GMP. When reconstituted with heme, it enables <em>c</em>-di-GMP synthesis, and depending on the redox state the synthesis rate is changed. To our knowledge, this is the first heme-dependent activity reported for a <em>c</em>-di-GMP-metabolizing enzyme in <em>Streptomyces</em> and has major implications for understanding the way <em>c</em>-di-GMP is metabolized <em>in vivo</em> in <em>Streptomyces</em>.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"269 ","pages":"Article 112874"},"PeriodicalIF":3.8,"publicationDate":"2025-02-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143561858","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}