JBIC Journal of Biological Inorganic Chemistry最新文献

{"title":"Research on synthesis and property of nano-textured Sc2O3-MgO efficient antibacterial agents","authors":"Ying Wang,&nbsp;Yanjing Liu,&nbsp;Xiyue Li,&nbsp;Yuezhou Liu,&nbsp;Fuming Wang,&nbsp;Yaping Huang,&nbsp;Bing Du,&nbsp;Yongfang Qian,&nbsp;Lihua Lv","doi":"10.1007/s00775-023-01995-2","DOIUrl":"10.1007/s00775-023-01995-2","url":null,"abstract":"<div><p>In order to obtain the inorganic efficient antibacterial agents, the means of ion doping and morphology construction in this research are used to enhance the antibacterial property of nano-MgO, which is according to the “oxidative damage mechanism” and “contact mechanism”. In this work, the nano-textured Sc₂O₃-MgO are synthesized by doping Sc³⁺ in nano-MgO lattice through calcining at 600 °C. When the Sc³⁺ content reaches 10%, the nanotextures on the powders surface are pretty clearly visible and uniform, and the specific surface area and the oxygen vacancy are ideal, so that the 10% Sc³⁺-doped powders (SM-10) has the excellent antibacterial property against <i>E. coli</i> and <i>S. aureus</i> (MBC = 0.03 mg/mL). The efficient antibacterial agents in this research have a better antibacterial effect than the 0% Sc³⁺-doped powders (SM-0, MBC = 0.20 mg/mL) and the commercial nano-MgO (CM, MBC = 0.40 mg/mL), which have application prospects in the field of antibacterial.</p></div>","PeriodicalId":603,"journal":{"name":"JBIC Journal of Biological Inorganic Chemistry","volume":"28 3","pages":"329 - 343"},"PeriodicalIF":3.0,"publicationDate":"2023-03-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-023-01995-2.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4263065","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}

{"title":"A personal account on 25 years of scientific literature on [FeFe]-hydrogenase","authors":"Jason W. Sidabras,&nbsp;Sven T. Stripp","doi":"10.1007/s00775-023-01992-5","DOIUrl":"10.1007/s00775-023-01992-5","url":null,"abstract":"<div><p>[FeFe]-hydrogenases are gas-processing metalloenzymes that catalyze H₂ oxidation and proton reduction (H₂ release) in microorganisms. Their high turnover frequencies and lack of electrical overpotential in the hydrogen conversion reaction has inspired generations of biologists, chemists, and physicists to explore the inner workings of [FeFe]-hydrogenase. Here, we revisit 25?years of scientific literature on [FeFe]-hydrogenase and propose a personal account on ‘must-read’ research papers and review article that will allow interested scientists to follow the recent discussions on catalytic mechanism, O₂ sensitivity, and the in vivo synthesis of the active site cofactor with its biologically uncommon ligands?carbon monoxide and cyanide. Focused on—but not restricted to—structural biology and molecular biophysics, we highlight future directions that may inspire young investigators to pursue a career in the exciting and competitive field of [FeFe]-hydrogenase research.</p><h3>Graphical abstract</h3>\u0000 <figure><div><div><div><picture><source><img></source></picture></div></div></div></figure>\u0000 </div>","PeriodicalId":603,"journal":{"name":"JBIC Journal of Biological Inorganic Chemistry","volume":"28 4","pages":"355 - 378"},"PeriodicalIF":3.0,"publicationDate":"2023-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-023-01992-5.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4044395","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}

{"title":"Histidine oxidation in lytic polysaccharide monooxygenase","authors":"Magne Torbjörnsson,&nbsp;Marlisa M. Hagemann,&nbsp;Ulf Ryde,&nbsp;Erik Donovan Hedegård","doi":"10.1007/s00775-023-01993-4","DOIUrl":"10.1007/s00775-023-01993-4","url":null,"abstract":"<div><p>The lytic polysaccharide monooxygenases (LPMOs) comprise a super-family of copper enzymes that boost the depolymerisation of polysaccharides by oxidatively disrupting the glycosidic bonds connecting the sugar units. Industrial use of LPMOs for cellulose depolymerisation has already begun but is still far from reaching its full potential. One issue is that the LPMOs self-oxidise and thereby deactivate. The mechanism of this self-oxidation is unknown, but histidine residues coordinating to the copper atom are the most susceptible. An unusual methyl modification of the NE2 atom in one of the coordinating histidine residues has been proposed to have a protective role. Furthermore, substrate binding is also known to reduce oxidative damage. We here for the first time investigate the mechanism of histidine oxidation with combined quantum and molecular mechanical (QM/MM) calculations, with outset in intermediates previously shown to form from a reaction with peroxide and a reduced LPMO. We show that an intermediate with a [Cu–O]^<b>+</b> moiety is sufficiently potent to oxidise the nearest C–H bond on both histidine residues, but methylation of the NE2 atom of His-1 increases the reaction barrier of this reaction. The substrate further increases the activation barrier. We also investigate a [Cu–OH]^2<b>+</b> intermediate with a deprotonated tyrosine radical. This intermediate was previously proposed to have a protective role, and we also find it to have higher barriers than the corresponding a [Cu–O]^<b>+</b> intermediate.</p><h3>Graphical abstract</h3>\u0000 <figure><div><div><div><picture><source><img></source></picture></div></div></div></figure>\u0000 </div>","PeriodicalId":603,"journal":{"name":"JBIC Journal of Biological Inorganic Chemistry","volume":"28 3","pages":"317 - 328"},"PeriodicalIF":3.0,"publicationDate":"2023-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-023-01993-4.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4964400","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}

{"title":"Zinc binding of a Cys2His2-type zinc finger protein is enhanced by the interaction with DNA","authors":"Bálint Hajdu,&nbsp;Éva Hunyadi-Gulyás,&nbsp;Kohsuke Kato,&nbsp;Atsushi Kawaguchi,&nbsp;Kyosuke Nagata,&nbsp;Béla Gyurcsik","doi":"10.1007/s00775-023-01988-1","DOIUrl":"10.1007/s00775-023-01988-1","url":null,"abstract":"<p>Zinc finger proteins specifically recognize DNA sequences and, therefore, play a crucial role in living organisms. In this study the Zn(II)-, and DNA-binding of 1MEY#, an artificial zinc finger protein consisting of three finger units was characterized by multiple methods. Fluorimetric, circular dichroism and isothermal calorimetric titrations were applied to determine the accurate stability constant of a zinc finger protein. Assuming that all three zinc finger subunits behave identically, the obtained thermodynamic data for the Zn(II) binding were <i>ΔH</i>_{binding site} =  − (23.5 − 28.0) kcal/mol (depending on the applied protonation state of the cysteines) and log<i>β</i>’_pH 7.4 = 12.2 ± 0.1, being similar to those of the CP1 consensus zinc finger peptide. The specific DNA binding of the protein can be characterized by log<i>β</i>’_{pH 7.4} = 8.20 ± 0.08, which is comparable to the affinity of the natural zinc finger proteins (Sp1, WT1, TFIIIA) toward DNA. This value is ~ 1.9 log<i>β</i>’ unit higher than those determined for semi- or nonspecific DNA binding. Competitive circular dichroism and electrophoretic mobility shift measurements revealed that the conditional stability constant characteristic for Zn(II) binding of 1MEY# protein increased by 3.4 orders of magnitude in the presence of its target DNA sequence.</p>","PeriodicalId":603,"journal":{"name":"JBIC Journal of Biological Inorganic Chemistry","volume":"28 3","pages":"301 - 315"},"PeriodicalIF":3.0,"publicationDate":"2023-02-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-023-01988-1.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4888815","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}

{"title":"Cyanide replaces substrate in obligate-ordered addition of nitric oxide to the non-heme mononuclear iron AvMDO active site","authors":"Nicholas J. York,&nbsp;Molly M. Lockart,&nbsp;Allison N. Schmittou,&nbsp;Brad S. Pierce","doi":"10.1007/s00775-023-01990-7","DOIUrl":"10.1007/s00775-023-01990-7","url":null,"abstract":"<div><p>Thiol dioxygenases are a subset of non-heme mononuclear iron oxygenases that catalyze the O₂-dependent oxidation of thiol-bearing substrates to yield sulfinic acid products. Cysteine dioxygenase (CDO) and 3-mercaptopropionic acid (<b>3MPA</b>) dioxygenase (MDO) are the most extensively characterized members of this enzyme family. As with many non-heme mononuclear iron oxidase/oxygenases, CDO and MDO exhibit an obligate-ordered addition of organic substrate before dioxygen. As this substrate-gated O₂-reactivity extends to the oxygen-surrogate, nitric oxide (NO), EPR spectroscopy has long been used to interrogate the [substrate:NO:enzyme] ternary complex. In principle, these studies can be extrapolated to provide information about transient iron-oxo intermediates produced during catalytic turnover with dioxygen. In this work, we demonstrate that cyanide mimics the native thiol-substrate in ordered-addition experiments with MDO cloned from <i>Azotobacter vinelandii</i> (<i>Av</i>MDO). Following treatment of the catalytically active Fe(II)-<i>Av</i>MDO with excess cyanide, addition of NO yields a low-spin (<i>S</i> = 1/2) (CN/NO)-Fe-complex. Continuous wave and pulsed X-band EPR characterization of this complex produced in wild-type and H157N variant <i>Av</i>MDO reveal multiple nuclear hyperfine features diagnostic of interactions within the first- and outer-coordination sphere of the enzymatic Fe-site. Spectroscopically validated computational models indicate simultaneous coordination of two cyanide ligands replaces the bidentate (thiol and carboxylate) coordination of <b>3MPA</b> allowing for NO-binding at the catalytically relevant O₂-binding site. This promiscuous substrate-gated reactivity of <i>Av</i>MDO with NO provides an instructive counterpoint to the high substrate-specificity exhibited by mammalian CDO for <span>l</span>-cysteine.</p><h3>Graphical abstract</h3>\u0000 <figure><div><div><div><picture><source><img></source></picture></div></div></div></figure>\u0000 </div>","PeriodicalId":603,"journal":{"name":"JBIC Journal of Biological Inorganic Chemistry","volume":"28 3","pages":"285 - 299"},"PeriodicalIF":3.0,"publicationDate":"2023-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-023-01990-7.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4817909","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}

{"title":"Tumor selective Ru(III) Schiff bases complexes with strong in vitro activity toward cisplatin-resistant MDA-MB-231 breast cancer cells","authors":"Marijana Pavlović,&nbsp;Emira Kahrović,&nbsp;Sandra Aranđelović,&nbsp;Siniša Radulović,&nbsp;Predrag-Peter Ilich,&nbsp;Sanja Grgurić-Šipka,&nbsp;Nevzeta Ljubijankić,&nbsp;Dijana Žilić,&nbsp;Jurica Jurec","doi":"10.1007/s00775-023-01989-0","DOIUrl":"10.1007/s00775-023-01989-0","url":null,"abstract":"<div><p>Novel ruthenium(III) complexes of general formula Na[RuCl₂(L¹⁻³-N,O)₂] where L^(1–3) denote deprotonated Schiff bases (HL¹-HL³) derived from 5-substituted salicyladehyde and alkylamine (propyl- or butylamine) were prepared and characterized based on elemental analysis, mass spectra, infrared, electron spin/paramagnetic resonance (ESR/EPR) spectroscopy, and cyclovoltammetric study. Optimization of five isomers of complex C1 was done by DFT calculation. The interaction of <b>C1</b>–<b>C3</b> complexes with DNA (Deoxyribonucleic acid) and BSA (Bovine serum albumin) was investigated by electron spectroscopy and fluorescence quenching. The cytotoxic activity of <b>C1</b>–<b>C3</b> was investigated in a panel of four human cancer cell lines (K562, A549, EA.hy926, MDA-MB-231) and one human non-tumor cell line (MRC-5). Complexes displayed an apparent cytoselective profile, with IC₅₀ values in the low micromolar range from 1.6 ± 0.3 to 23.0 ± 0.1 µM. Cisplatin-resistant triple-negative breast cancer cells MDA-MB-231 displayed the highest sensitivity to complexes, with Ru(III) compound containing two chlorides and two deprotonated <i>N</i>-propyl-5-chloro-salicylidenimine (hereinafter <b>C1</b>) as the most potent (IC₅₀ = 1.6 µM), and approximately ten times more active than cisplatin (IC₅₀ = 21.9 µM). MDA-MB-231 cells treated for 24 h with <b>C1</b> presented with apoptotic morphology, as seen by acridine orange/ethidium bromide staining, while 48 h of treatment induced DNA fragmentation, and necrotic changes in cells, as seen by flow cytometry analysis. Drug-accumulation study by inductively coupled plasma mass spectrometry (ICP-MS) demonstrated markedly higher intracellular accumulation of <b>C1</b> compared with cisplatin.</p><h3>Graphical abstract</h3>\u0000 <figure><div><div><div><picture><source><img></source></picture></div></div></div></figure>\u0000 </div>","PeriodicalId":603,"journal":{"name":"JBIC Journal of Biological Inorganic Chemistry","volume":"28 3","pages":"263 - 284"},"PeriodicalIF":3.0,"publicationDate":"2023-02-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-023-01989-0.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4530945","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}

{"title":"Associations between Relationship Status, Anxiety, Sexual Function, and Sexual Satisfaction in Lesbian, Gay, and Bisexual People.","authors":"Elizabeth Arthur, Kathryn Flynn, Diana Jeffery, Rachel Cusatis","doi":"10.1080/19317611.2023.2172510","DOIUrl":"10.1080/19317611.2023.2172510","url":null,"abstract":"<p><strong>Objectives: </strong>The purpose of this study was to describe associations between relationship status, anxiety, and sexual function and satisfaction in lesbian, gay, and bisexual (LGB) adults.</p><p><strong>Methods: </strong>Linear regression determined associations between sexual function, relationship characteristics and anxiety in 979 LGB participants.</p><p><strong>Results: </strong>Relationship status was not related to sexual interest in gay men. Partnered relationship status was associated with higher sexual satisfaction for gay men, lesbians, and bisexual women. Anxiety symptoms were negatively associated with sexual interest, satisfaction, and orgasm pleasure for gay men but not associated with sexual outcomes in lesbian women.</p><p><strong>Conclusion: </strong>Using a nationally representative sample of LGB adults, differences were found in factors related to sexual function and satisfaction by gender and sexual orientation.</p>","PeriodicalId":603,"journal":{"name":"JBIC Journal of Biological Inorganic Chemistry","volume":"25 6","pages":"41-51"},"PeriodicalIF":2.0,"publicationDate":"2023-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10903708/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41294967","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}

{"title":"The past, present, and future of artificial zinc finger proteins: design strategies and chemical and biological applications","authors":"Shigeru Negi,&nbsp;Miki Imanishi,&nbsp;Mami Hamori,&nbsp;Yuka Kawahara-Nakagawa,&nbsp;Wataru Nomura,&nbsp;Kanae Kishi,&nbsp;Nobuhito Shibata,&nbsp;Yukio Sugiura","doi":"10.1007/s00775-023-01991-6","DOIUrl":"10.1007/s00775-023-01991-6","url":null,"abstract":"<div><p>Zinc finger proteins are abundant in the human proteome and are responsible for a variety of functions. The domains that constitute zinc finger proteins are compact spherical structures, each comprising approximately 30 amino acid residues, but they also have precise molecular factor functions: zinc binding and DNA recognition. Due to the biological importance of zinc finger proteins and their unique structural and functional properties, many artificial zinc finger proteins have been created and are expected to improve their functions and biological applications. In this study, we review previous studies on the redesign and application of artificial zinc finger proteins, focusing on the experimental results obtained by our research group. In addition, we systematically review various design strategies used to construct artificial zinc finger proteins and discuss in detail their potential biological applications, including gene editing. This review will provide relevant information to researchers involved or interested in the field of artificial zinc finger proteins as a potential new treatment for various diseases.</p></div>","PeriodicalId":603,"journal":{"name":"JBIC Journal of Biological Inorganic Chemistry","volume":"28 3","pages":"249 - 261"},"PeriodicalIF":3.0,"publicationDate":"2023-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-023-01991-6.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4293721","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}

{"title":"Synthesis, structural characterization and study of antioxidant and anti-PrPSc properties of flavonoids and their rhenium(I)–tricarbonyl complexes","authors":"Pigi Glykofridi,&nbsp;Vassiliki-Eleni Tziouri,&nbsp;Konstantinos Xanthopoulos,&nbsp;Maria-Eirini Vlachou,&nbsp;Susana Correia,&nbsp;Anna-Lisa Fischer,&nbsp;Katrin Thüne,&nbsp;Antonios Hatzidimitriou,&nbsp;Inga Zerr,&nbsp;Matthias Schmitz,&nbsp;Theodoros Sklaviadis,&nbsp;Dimitra Hadjipavlou-Litina,&nbsp;Dionysia Papagiannopoulou","doi":"10.1007/s00775-022-01986-9","DOIUrl":"10.1007/s00775-022-01986-9","url":null,"abstract":"<div><p>This study aims at the synthesis and initial biological evaluation of novel rhenium–tricarbonyl complexes of 3,3′,4′,5,7-pentahydroxyflavone (quercetin), 3,7,4΄-trihydroxyflavone (resokaempferol), 5,7-dihydroxyflavone (chrysin) and 4΄,5,7-trihydroxyflavonone (naringenin) as neuroprotective and anti-PrP agents. Resokaempferol was synthesized from 2,2΄,4-trihydroxychalcone by H₂O₂/NaOH. The rhenium–tricarbonyl complexes of the type <i>fac</i>-[Re(CO)₃(Fl)(sol)] were synthesized by reacting the precursor <i>fac</i>-[Re(CO)₃(sol)₃]⁺ with an equimolar amount of the flavonoids (Fl) quercetin, resokaempferol, chrysin and naringenin and the solvent (sol) was methanol or water. The respective Re–flavonoid complexes were purified by semi-preparative HPLC and characterized by spectroscopic methods. Furthermore, the structure of Re–chrysin was elucidated by X-ray crystallography. Initial screening of the neuroprotective properties of these compounds included the in vitro assessment of the antioxidant properties by the DPPH assay as well as the anti-lipid peroxidation of linoleic acid in the presence of AAPH and their ability to inhibit soybean lipoxygenase. From the above studies, it was concluded that the complexes’ properties are mainly correlated with the structural characteristics and the presence of the flavonoids. The flavonoids and their respective Re-complexes were also tested in vitro for their ability to inhibit the formation and aggregation of the amyloid-like abnormal prion protein, PrP^Sc, by employing the real-time quaking-induced conversion assay with recombinant PrP seeded with cerebrospinal fluid from patients with Creutzfeldt–Jakob disease. All the compounds blocked de novo abnormal PrP formation and aggregation.</p><h3>Graphical abstract</h3>\u0000 <figure><div><div><div><picture><source><img></source></picture></div></div></div></figure>\u0000 </div>","PeriodicalId":603,"journal":{"name":"JBIC Journal of Biological Inorganic Chemistry","volume":"28 2","pages":"235 - 247"},"PeriodicalIF":3.0,"publicationDate":"2023-01-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-022-01986-9.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4966387","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}

{"title":"Gold drugs as colistin adjuvants in the fight against MCR-1 producing bacteria","authors":"Qi Zhang,&nbsp;Minji Wang,&nbsp;Xuqiao Hu,&nbsp;Aixin Yan,&nbsp;Pak-Leung Ho,&nbsp;Hongyan Li,&nbsp;Hongzhe Sun","doi":"10.1007/s00775-022-01983-y","DOIUrl":"10.1007/s00775-022-01983-y","url":null,"abstract":"<div><p>The emergence and rapid spread of the mobile colistin resistance gene <i>mcr-1</i> among bacterial species and hosts significantly challenge the efficacy of “last-line” antibiotic colistin. Previously, we reported silver nitrate and auranofin serve as colistin adjuvants for combating <i>mcr-1</i>-positive bacteria. Herein, we uncovered more gold-based drugs and nanoparticles, and found that they exhibited varying degree of synergisms with colistin on killing <i>mcr-1</i>-positive bacteria. However, pre-activation of the drugs by either glutathione or <i>N</i>-acetyl cysteine, thus releasing and accumulating gold ions, is perquisite for their abilities to substitute zinc cofactor from MCR-1 enzyme. X-ray crystallography and biophysical studies further supported the proposed mechanism. This study not only provides basis for combining gold-based drugs and colistin for combating <i>mcr-1</i>-positive bacterial infections, but also undoubtedly opens a new horizon for metabolism details of gold-based drugs in overcoming antimicrobial resistance.</p><h3>Graphical abstract</h3>\u0000 <figure><div><div><div><picture><source><img></source></picture></div></div></div></figure>\u0000 </div>","PeriodicalId":603,"journal":{"name":"JBIC Journal of Biological Inorganic Chemistry","volume":"28 2","pages":"225 - 234"},"PeriodicalIF":3.0,"publicationDate":"2023-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4788435","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}