{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,28]],"date-time":"2026-10-28T23:19:25Z","timestamp":1793229565953,"version":"4.5.0"},"reference-count":64,"publisher":"American Chemical Society (ACS)","issue":"12","license":[{"start":{"date-parts":[[2015,10,13]],"date-time":"2015-10-13T00:00:00Z","timestamp":1444694400000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,12,16]]},"abstract":"<jats:title>Conspectus<\/jats:title>\n                  <jats:p>The human innate immune system has evolved the means to reduce the bioavailability of first-row late d-block transition metal ions to invading microbial pathogens in a process termed \u201cnutritional immunity\u201d. Transition metals from Mn(II) to Zn(II) function as metalloenzyme cofactors in all living cells, and the successful pathogen is capable of mounting an adaptive response to mitigate the effects of host control of transition metal bioavailability. Emerging evidence suggests that Mn, Fe, and Zn are withheld from the pathogen in classically defined nutritional immunity, while Cu is used to kill invading microorganisms. This Account summarizes new molecular-level insights into copper trafficking across cell membranes from studies of a number of important bacterial pathogens and model organisms, including Escherichia coli, Salmonella species, Mycobacterium tuberculosis, and Streptococcus pneumoniae, to illustrate general principles of cellular copper resistance.<\/jats:p>\n                  <jats:p>Recent highlights of copper chemistry at the host\u2013microbial pathogen interface include the first high resolution structures and functional characterization of a Cu(I)-effluxing P1B-ATPase, a new class of bacterial copper chaperone, a fungal Cu-only superoxide dismutase SOD5, and the discovery of a small molecule Cu-bound SOD mimetic. Successful harnessing by the pathogen of host-derived bactericidal Cu to reduce the bacterial load of reactive oxygen species (ROS) is an emerging theme; in addition, recent studies continue to emphasize the importance of short lifetime protein\u2013protein interactions that orchestrate the channeling of Cu(I) from donor to target without dissociation into bulk solution; this, in turn, mitigates the off-pathway effects of Cu(I) toxicity in both the periplasm in Gram negative organisms and in the bacterial cytoplasm. It is unclear as yet, outside of the photosynthetic bacteria, whether Cu(I) is trafficked to other cellular destinations, for example, to cuproenzymes or other intracellular storage sites, or the general degree to which copper chaperones vs copper efflux transporters are essential for bacterial pathogenesis in the vertebrate host.<\/jats:p>\n                  <jats:p>Future studies will be directed toward the identification and structural characterization of other cellular targets of Cu(I) trafficking and resistance, the physical and mechanistic characterization of Cu(I)-transfer intermediates, and elucidation of the mutual dependence of Cu(I) trafficking and cellular redox status on thiol chemistry in the cytoplasm. Crippling bacterial control of Cu(I) sensing, trafficking, and efflux may represent a viable strategy for the development of new antibiotics.<\/jats:p>","DOI":"10.1021\/ar500300n","type":"journal-article","created":{"date-parts":[[2014,10,13]],"date-time":"2014-10-13T16:22:17Z","timestamp":1413217337000},"page":"3605-3613","source":"Crossref","is-referenced-by-count":140,"title":["Copper Transport and Trafficking\nat the Host\u2013Bacterial\nPathogen Interface"],"prefix":"10.1021","volume":"47","author":[{"given":"Yue","family":"Fu","sequence":"first","affiliation":[{"name":"Indiana University , , , ,","place":["Bloomington, Indiana, United States, 47405-7102"]},{"name":"Indiana University , , , ,","place":["Bloomington, Indiana, United States, 47405"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Feng-Ming James","family":"Chang","sequence":"additional","affiliation":[{"name":"Indiana University , , , ,","place":["Bloomington, Indiana, United States, 47405-7102"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David P.","family":"Giedroc","sequence":"additional","affiliation":[{"name":"Indiana University , , , ,","place":["Bloomington, Indiana, United States, 47405-7102"]},{"name":"Indiana University , , , ,","place":["Bloomington, Indiana, United States, 47405"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,10,13]]},"reference":[{"key":"2026090400152634200_cit1","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.cbpa.2013.12.021","article-title":"Recent developments in copper and zinc homeostasis\nin bacterial pathogens","volume":"19","author":"Braymer","year":"2014","journal-title":"Curr. Opin. Chem. Biol."},{"key":"2026090400152634200_cit2","doi-asserted-by":"crossref","first-page":"3","DOI":"10.3389\/fcimb.2014.00003","article-title":"Pathogenic\nadaptations to host-derived antibacterial\ncopper","volume":"4","author":"Chaturvedi","year":"2014","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"2026090400152634200_cit3","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.chom.2012.01.009","article-title":"Copper in microbial\npathogenesis: Meddling with the metal","volume":"11","author":"Samanovic","year":"2012","journal-title":"Cell\nHost Microbe"},{"key":"2026090400152634200_cit4","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.jinorgbio.2011.11.024","article-title":"Coordination chemistry\nof copper proteins: How nature\nhandles a toxic cargo for essential function","volume":"107","author":"Rubino","year":"2012","journal-title":"J. Inorg. Biochem."},{"key":"2026090400152634200_cit5","doi-asserted-by":"crossref","first-page":"1616","DOI":"10.1128\/JB.01357-06","article-title":"Intracellular copper does not catalyze\nthe formation of oxidative DNA damage in Escherichia coli","volume":"189","author":"Macomber","year":"2007","journal-title":"J. Bacteriol."},{"key":"2026090400152634200_cit6","doi-asserted-by":"crossref","first-page":"8344","DOI":"10.1073\/pnas.0812808106","article-title":"The iron-sulfur clusters of dehydratases are primary\nintracellular targets of copper toxicity","volume":"106","author":"Macomber","year":"2009","journal-title":"Proc.\nNatl. Acad. Sci. U. S. A."},{"key":"2026090400152634200_cit7","doi-asserted-by":"crossref","first-page":"2512","DOI":"10.1128\/JB.00058-10","article-title":"Copper stress affects iron homeostasis by destabilizing\niron-sulfur cluster formation in Bacillus subtilis","volume":"192","author":"Chillappagari","year":"2010","journal-title":"J. Bacteriol."},{"key":"2026090400152634200_cit8","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1111\/mmi.12188","article-title":"Coproporphyrin\nIII excretion identifies the anaerobic coproporphyrinogen III oxidase\nHemN as a copper target in the Cu(+)-ATPase mutant copA(\u2212) of Rubrivivax gelatinosus","volume":"88","author":"Azzouzi","year":"2013","journal-title":"Mol. Microbiol."},{"key":"2026090400152634200_cit9","doi-asserted-by":"crossref","first-page":"2217","DOI":"10.1021\/cb4002443","article-title":"Antimicrobial action of copper is amplified via inhibition\nof heme biosynthesis","volume":"8","author":"Djoko","year":"2013","journal-title":"ACS Chem. Biol."},{"key":"2026090400152634200_cit10","doi-asserted-by":"crossref","first-page":"6390","DOI":"10.1128\/JB.00995-10","article-title":"Instability of ackA\n(acetate kinase) mutations and their effects on acetyl phosphate and\nATP amounts in Streptococcus pneumoniae D39","volume":"192","author":"Ramos-Montanez","year":"2010","journal-title":"J. Bacteriol."},{"key":"2026090400152634200_cit11","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.cbpa.2010.01.003","article-title":"Human copper\nhomeostasis: A network of interconnected pathways","volume":"14","author":"Lutsenko","year":"2010","journal-title":"Curr. .Opin. Chem. Biol."},{"key":"2026090400152634200_cit12","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1126\/science.284.5415.805","article-title":"Undetectable\nintracellular free copper: The Requirement of a copper chaperone for\nsuperoxide dismutase","volume":"284","author":"Rae","year":"1999","journal-title":"Science"},{"key":"2026090400152634200_cit13","doi-asserted-by":"crossref","first-page":"4760","DOI":"10.1021\/cr900104z","article-title":"Structural\nbiology of copper trafficking","volume":"109","author":"Boal","year":"2009","journal-title":"Chem. Rev."},{"key":"2026090400152634200_cit14","doi-asserted-by":"crossref","first-page":"3081","DOI":"10.1021\/ja0390350","article-title":"C-terminal\ndomain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu(I) ions as a cuprous-thiolate polynuclear\ncluster: Sub-femtomolar Cu(I) affinity of three proteins involved\nin copper trafficking","volume":"126","author":"Xiao","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"2026090400152634200_cit15","doi-asserted-by":"crossref","first-page":"C768","DOI":"10.1152\/ajpcell.00417.2012","article-title":"Cellular\nglutathione plays a key\nrole in copper uptake mediated by human copper transporter 1","volume":"304","author":"Maryon","year":"2013","journal-title":"Am. J. Physiol.: Cell Physiol."},{"key":"2026090400152634200_cit16","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1007\/s00232-013-9592-1","article-title":"Atox1 contains positive residues that mediate membrane association\nand aid subsequent copper loading","volume":"246","author":"Flores","year":"2013","journal-title":"J. Membr.\nBiol."},{"key":"2026090400152634200_cit17","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1038\/nchembio.1168","article-title":"A new structural\nparadigm in copper\nresistance in Streptococcus pneumoniae","volume":"9","author":"Fu","year":"2013","journal-title":"Nat. Chem. Biol."},{"key":"2026090400152634200_cit18","doi-asserted-by":"crossref","first-page":"33949","DOI":"10.1074\/jbc.M109.070201","article-title":"A role for the ATP7A\ncopper-transporting ATPase in macrophage bactericidal activity","volume":"284","author":"White","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2026090400152634200_cit19","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.00876-13","article-title":"The copper-responsive\nRicR regulon contributes to Mycobacterium tuberculosis virulence","volume":"5","author":"Shi","year":"2014","journal-title":"mBio"},{"key":"2026090400152634200_cit20","doi-asserted-by":"crossref","first-page":"1621","DOI":"10.1073\/pnas.1009261108","article-title":"Copper resistance is essential for\nvirulence of Mycobacterium tuberculosis","volume":"108","author":"Wolschendorf","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026090400152634200_cit21","doi-asserted-by":"crossref","first-page":"1923","DOI":"10.1002\/eji.200738056","article-title":"Interferon-gamma limits the availability\nof iron for intramacrophage Salmonellta typhimurium","volume":"38","author":"Nairz","year":"2008","journal-title":"Eur. J. Immunol."},{"key":"2026090400152634200_cit22","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1038\/nchembio.1020","article-title":"The siderophore yersiniabactin binds copper to protect\npathogens during infection","volume":"8","author":"Chaturvedi","year":"2012","journal-title":"Nat. Chem. Biol."},{"key":"2026090400152634200_cit23","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1021\/cb400658k","article-title":"Cupric\nyersiniabactin is a virulence-associated superoxide dismutase mimic","volume":"9","author":"Chaturvedi","year":"2014","journal-title":"ACS Chem. Biol."},{"key":"2026090400152634200_cit24","doi-asserted-by":"crossref","first-page":"5866","DOI":"10.1073\/pnas.1400137111","article-title":"Candida albicans SOD5 represents the\nprototype of an unprecedented class of Cu-only superoxide dismutases\nrequired for pathogen defense","volume":"111","author":"Gleason","year":"2014","journal-title":"Proc. Natl. Acad.\nSci. U. S. A."},{"key":"2026090400152634200_cit25","doi-asserted-by":"crossref","first-page":"33447","DOI":"10.1074\/jbc.M404699200","article-title":"Unique features of the sodC-encoded superoxide dismutase\nfrom Mycobacterium tuberculosis, a fully functional\ncopper-containing enzyme lacking zinc in the active site","volume":"279","author":"Spagnolo","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2026090400152634200_cit26","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1093\/glycob\/cwn102","article-title":"N-Terminal clustering of the O-glycosylation sites\nin the Mycobacterium tuberculosis lipoprotein SodC","volume":"19","author":"Sartain","year":"2009","journal-title":"Glycobiology"},{"key":"2026090400152634200_cit27","doi-asserted-by":"crossref","first-page":"5133","DOI":"10.1128\/JB.00763-13","article-title":"Porins increase copper susceptibility of Mycobacterium tuberculosis","volume":"195","author":"Speer","year":"2013","journal-title":"J. Bacteriol."},{"key":"2026090400152634200_cit28","doi-asserted-by":"crossref","first-page":"2362","DOI":"10.1128\/JB.01616-08","article-title":"Copper\nacquisition is mediated by YcnJ and regulated by YcnK and CsoR in Bacillus subtilis","volume":"191","author":"Chillappagari","year":"2009","journal-title":"J. Bacteriol."},{"key":"2026090400152634200_cit29","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1039\/c1mt00107h","article-title":"Copper toxicity\nand the origin of\nbacterial resistance-new insights and applications","volume":"3","author":"Dupont","year":"2011","journal-title":"Metallomics"},{"key":"2026090400152634200_cit30","doi-asserted-by":"crossref","first-page":"4644","DOI":"10.1021\/cr900077w","article-title":"Coordination chemistry of bacterial\nmetal transport and sensing","volume":"109","author":"Ma","year":"2009","journal-title":"Chem. Rev."},{"key":"2026090400152634200_cit31","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1098\/rstb.2011.0203","article-title":"Structure and mechanism\nof the tripartite CusCBA heavy-metal efflux\ncomplex","volume":"367","author":"Long","year":"2012","journal-title":"Philos. Trans. R. Soc. London, Ser.\nB: Biol. Sci."},{"key":"2026090400152634200_cit32","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/B978-0-12-394390-3.00007-0","article-title":"Metal export by CusCFBA, the periplasmic\nCu(I)\/Ag(I) transport system of Escherichia coli","volume":"69","author":"Mealman","year":"2012","journal-title":"Curr. Top. Membr."},{"key":"2026090400152634200_cit33","doi-asserted-by":"crossref","first-page":"3804","DOI":"10.1128\/JB.185.13.3804-3812.2003","article-title":"Molecular analysis\nof the copper-transporting efflux system CusCFBA of Escherichia coli","volume":"185","author":"Franke","year":"2003","journal-title":"J. Bacteriol."},{"key":"2026090400152634200_cit34","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1038\/nchembio.2007.57","article-title":"Cu(I) recognition via cation-\u03c0 and methionine\ninteractions in CusF","volume":"4","author":"Xue","year":"2008","journal-title":"Nat. Chem. Biol."},{"key":"2026090400152634200_cit35","doi-asserted-by":"crossref","first-page":"11408","DOI":"10.1021\/bi801638m","article-title":"Direct metal transfer\nbetween periplasmic proteins identifies a bacterial copper chaperone","volume":"47","author":"Bagai","year":"2008","journal-title":"Biochemistry"},{"key":"2026090400152634200_cit36","doi-asserted-by":"crossref","first-page":"2559","DOI":"10.1021\/bi102012j","article-title":"Interactions between\nCusF and CusB identified by NMR spectroscopy and chemical cross-linking\ncoupled to mass spectrometry","volume":"50","author":"Mealman","year":"2011","journal-title":"Biochemistry"},{"key":"2026090400152634200_cit37","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.1411475111","article-title":"Tracking\nmetal ions through a Cu\/Ag efflux pump assigns the functional roles\nof the periplasmic proteins","author":"Chacon","year":"2014","journal-title":"Proc. Natl. Acad.\nSci. U. S. A."},{"key":"2026090400152634200_cit38","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1038\/nchembio0308-148","article-title":"A place for thioether chemistry in cellular copper\nion recognition and trafficking","volume":"4","author":"Davis","year":"2008","journal-title":"Nat. Chem.\nBiol."},{"key":"2026090400152634200_cit39","doi-asserted-by":"crossref","first-page":"20492","DOI":"10.1074\/jbc.M114.577668","article-title":"Mechanism of ATPase-mediated\nCu+ export and delivery to periplasmic chaperones: The interaction\nof Escherichia coli CopA and CusF","volume":"289","author":"Padilla-Benavides","year":"2014","journal-title":"J. Biol. Chem."},{"key":"2026090400152634200_cit40","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1111\/j.1574-6968.2012.02529.x","article-title":"Regulation of Cu(I)\/Ag(I)\nefflux genes in Escherichia coli by the sensor kinase\nCusS","volume":"330","author":"Gudipaty","year":"2012","journal-title":"FEMS Microbiol. Lett."},{"key":"2026090400152634200_cit41","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1111\/j.1365-2958.2009.06763.x","article-title":"Alternative periplasmic copper-resistance\nmechanisms\nin Gram negative bacteria","volume":"73","author":"Pontel","year":"2009","journal-title":"Mol. Microbiol."},{"key":"2026090400152634200_cit42","doi-asserted-by":"crossref","first-page":"25259","DOI":"10.1074\/jbc.M110.145953","article-title":"Copper homeostasis\nin Salmonella is atypical and copper-CueP is a major\nperiplasmic metal complex","volume":"285","author":"Osman","year":"2010","journal-title":"J. Biol. Chem."},{"key":"2026090400152634200_cit43","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1111\/mmi.12107","article-title":"The copper supply pathway to a Salmonella Cu,Zn-superoxide dismutase (SodCII) involves\nP1B-type ATPase copper efflux and periplasmic CueP","volume":"87","author":"Osman","year":"2013","journal-title":"Mol. Microbiol."},{"key":"2026090400152634200_cit44","doi-asserted-by":"crossref","first-page":"5992","DOI":"10.1073\/pnas.0711446105","article-title":"Mechanism of Cu+-transporting ATPases: soluble Cu+\nchaperones directly transfer Cu+ to transmembrane transport sites","volume":"105","author":"Gonzalez-Guerrero","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2026090400152634200_cit45","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1073\/pnas.1117515109","article-title":"Cyanobacterial metallochaperone\ninhibits\ndeleterious side reactions of copper","volume":"109","author":"Tottey","year":"2012","journal-title":"Proc.\nNatl. Acad. Sci. U. S. A."},{"key":"2026090400152634200_cit46","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/S0378-1097(03)00095-8","article-title":"CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA","volume":"220","author":"Radford","year":"2003","journal-title":"FEMS Microbiol. Lett."},{"key":"2026090400152634200_cit47","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1111\/j.1365-2958.2011.07705.x","article-title":"The combined actions of the copper-responsive repressor\nCsoR and copper-metallochaperone CopZ modulate CopA-mediated copper\nefflux in the intracellular pathogen Listeria monocytogenes","volume":"81","author":"Corbett","year":"2011","journal-title":"Mol. Microbiol."},{"key":"2026090400152634200_cit48","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1111\/j.1365-2958.2011.07758.x","article-title":"The cop operon is required for copper\nhomeostasis and contributes\nto virulence in Streptococcus pneumoniae","volume":"81","author":"Shafeeq","year":"2011","journal-title":"Mol. Microbiol."},{"key":"2026090400152634200_cit49","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1039\/b906678k","article-title":"Molecular recognition\nin copper trafficking","volume":"27","author":"Banci","year":"2010","journal-title":"Nat. Prod. Rep."},{"key":"2026090400152634200_cit50","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1038\/nature10191","article-title":"Crystal structure\nof a copper-transporting\nPIB-type ATPase","volume":"475","author":"Gourdon","year":"2011","journal-title":"Nature"},{"key":"2026090400152634200_cit51","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1038\/nsmb.2721","article-title":"Copper-transporting\nP-type ATPases use a unique ion-release pathway","volume":"21","author":"Andersson","year":"2014","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026090400152634200_cit52","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1074\/jbc.M112.420810","article-title":"The mechanism of Cu+ transport ATPases:\nInteraction with Cu+ chaperones and the role of transient metal-binding\nsites","volume":"288","author":"Padilla-Benavides","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2026090400152634200_cit53","doi-asserted-by":"crossref","first-page":"29753","DOI":"10.1074\/jbc.M803248200","article-title":"Structure\nof the two transmembrane Cu+ transport sites of the Cu+-ATPases","volume":"283","author":"Gonzalez-Guerrero","year":"2008","journal-title":"J. Biol. Chem."},{"key":"2026090400152634200_cit54","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1038\/nrmicro2836","article-title":"Nutritional immunity: Transition metals at the pathogen\u2013host\ninterface","volume":"10","author":"Hood","year":"2012","journal-title":"Nat. Rev. Microbiol."},{"key":"2026090400152634200_cit55","doi-asserted-by":"crossref","first-page":"26678","DOI":"10.1074\/jbc.M112.381178","article-title":"Functional\npartnership of the copper export machinery and glutathione balance\nin human cells","volume":"287","author":"Hatori","year":"2012","journal-title":"J. Biol. Chem."},{"key":"2026090400152634200_cit56","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1039\/C4MT00020J","article-title":"Redox sulfur chemistry\nof the copper chaperone Atox1 is regulated by the enzyme glutaredoxin\n1, the reduction potential of the glutathione couple GSSG\/2GSH and\nthe availability of Cu(I)","volume":"6","author":"Brose","year":"2014","journal-title":"Metallomics"},{"key":"2026090400152634200_cit57","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1038\/nature09018","article-title":"Affinity gradients\ndrive copper to cellular destinations","volume":"465","author":"Banci","year":"2010","journal-title":"Nature"},{"key":"2026090400152634200_cit58","doi-asserted-by":"crossref","first-page":"5431","DOI":"10.1128\/JB.00271-08","article-title":"Glutathione and\ntransition-metal homeostasis in Escherichia coli","volume":"190","author":"Helbig","year":"2008","journal-title":"J. Bacteriol."},{"key":"2026090400152634200_cit59","doi-asserted-by":"crossref","first-page":"6248","DOI":"10.1128\/JB.01393-12","article-title":"Streptococcus pneumoniae uses glutathione to defend against oxidative stress and metal ion\ntoxicity","volume":"194","author":"Potter","year":"2012","journal-title":"J. Bacteriol."},{"key":"2026090400152634200_cit60","doi-asserted-by":"crossref","first-page":"3724","DOI":"10.1128\/JB.00546-13","article-title":"A multicopper oxidase is required\nfor copper resistance\nin Mycobacterium tuberculosis","volume":"195","author":"Rowland","year":"2013","journal-title":"J. Bacteriol."},{"key":"2026090400152634200_cit61","doi-asserted-by":"crossref","first-page":"1096","DOI":"10.1111\/j.1365-2958.2010.07273.x","article-title":"CtpV: A putative copper exporter required for full\nvirulence of Mycobacterium tuberculosis","volume":"77","author":"Ward","year":"2010","journal-title":"Mol. Microbiol."},{"key":"2026090400152634200_cit62","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1126\/science.1085950","article-title":"Molecular basis of metal-ion selectivity\nand zeptomolar sensitivity by CueR","volume":"301","author":"Changela","year":"2003","journal-title":"Science"},{"key":"2026090400152634200_cit63","doi-asserted-by":"crossref","first-page":"19204","DOI":"10.1074\/jbc.M114.556704","article-title":"Cu(I)-mediated\nallosteric switching in a copper-sensing operon repressor (CsoR)","volume":"289","author":"Chang","year":"2014","journal-title":"J. Biol. Chem."},{"key":"2026090400152634200_cit64","doi-asserted-by":"crossref","first-page":"5834","DOI":"10.1021\/ja058528x","article-title":"Intermolecular\ntransfer of copper ions from the CopC protein of Pseudomonas syringae. Crystal structures of fully loaded Cu(I)Cu(II)\nforms","volume":"128","author":"Zhang","year":"2006","journal-title":"J. Am. Chem. Soc."}],"container-title":["Accounts of Chemical Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/ar500300n","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/achre4\/article-pdf\/47\/12\/3605\/12052138\/ar500300n.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/achre4\/article-pdf\/47\/12\/3605\/12052138\/ar500300n.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,7]],"date-time":"2026-09-07T15:31:15Z","timestamp":1788795075000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/achre4\/article\/47\/12\/3605\/1248261\/Copper-Transport-and-Trafficking-at-the-Host"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,10,13]]},"references-count":64,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2014,10,13]]},"published-print":{"date-parts":[[2014,12,16]]}},"URL":"https:\/\/doi.org\/10.1021\/ar500300n","relation":{},"ISSN":["0001-4842","1520-4898"],"issn-type":[{"value":"0001-4842","type":"print"},{"value":"1520-4898","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,10,13]]}}}