{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,13]],"date-time":"2026-01-13T01:02:42Z","timestamp":1768266162073,"version":"3.49.0"},"reference-count":63,"publisher":"Elsevier BV","issue":"32","license":[{"start":{"date-parts":[[2020,8,1]],"date-time":"2020-08-01T00:00:00Z","timestamp":1596240000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,11,13]],"date-time":"2020-11-13T00:00:00Z","timestamp":1605225600000},"content-version":"vor","delay-in-days":104,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100012659","name":"NSF | Foundation for Innovative Research Groups of the National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31930003"],"award-info":[{"award-number":["31930003"]}],"id":[{"id":"10.13039\/501100012659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2020,8]]},"DOI":"10.1074\/jbc.ra120.014010","type":"journal-article","created":{"date-parts":[[2020,6,13]],"date-time":"2020-06-13T02:44:30Z","timestamp":1592016270000},"page":"11118-11130","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":19,"title":["Plasticity of the peroxidase AhpC links multiple substrates to diverse disulfide-reducing pathways in Shewanella oneidensis"],"prefix":"10.1016","volume":"295","author":[{"given":"Xue","family":"Feng","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kailun","family":"Guo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2647-6563","authenticated-orcid":false,"given":"Haichun","family":"Gao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA120.014010_bib1","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1515\/BC.2002.040","article-title":"Peroxiredoxins","volume":"383","author":"Hofmann","year":"2002","journal-title":"Biol. Chem"},{"key":"10.1074\/jbc.RA120.014010_bib2","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1007\/978-1-4020-6051-9_7","article-title":"Peroxiredoxins in bacterial antioxidant defense","volume":"44","author":"Dubbs","year":"2007","journal-title":"Subcell. Biochem"},{"key":"10.1074\/jbc.RA120.014010_bib3","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.abb.2004.09.006","article-title":"Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases","volume":"433","author":"Poole","year":"2005","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.RA120.014010_bib4","doi-asserted-by":"crossref","first-page":"13349","DOI":"10.1021\/bi9713658","article-title":"Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium","volume":"36","author":"Ellis","year":"1997","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.014010_bib5","doi-asserted-by":"crossref","first-page":"8859","DOI":"10.1021\/bi000826d","article-title":"Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but does not affect thioredoxin reductase activity","volume":"39","author":"Reynolds","year":"2000","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.014010_bib6","doi-asserted-by":"crossref","first-page":"5493","DOI":"10.1021\/bi012173m","article-title":"Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins","volume":"41","author":"Wood","year":"2002","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.014010_bib7","doi-asserted-by":"crossref","first-page":"1932","DOI":"10.1016\/j.bbabio.2014.08.007","article-title":"Key roles of the Escherichia coli AhpC C-terminus in assembly and catalysis of alkylhydroperoxide reductase, an enzyme essential for the alleviation of oxidative stress","volume":"1837","author":"Dip","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA120.014010_bib8","doi-asserted-by":"crossref","first-page":"1488","DOI":"10.1016\/S0021-9258(18)94214-6","article-title":"An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defense of DNA against oxidative damage: purification and properties","volume":"264","author":"Jacobson","year":"1989","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.014010_bib9","doi-asserted-by":"crossref","first-page":"2049","DOI":"10.1128\/jb.171.4.2049-2055.1989","article-title":"An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimuriumEscherichia coli: genetic characterization and cloning of ahp","volume":"171","author":"Storz","year":"1989","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA120.014010_bib10","doi-asserted-by":"crossref","first-page":"7173","DOI":"10.1128\/JB.183.24.7173-7181.2001","article-title":"Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli","volume":"183","author":"Seaver","year":"2001","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA120.014010_bib11","doi-asserted-by":"crossref","first-page":"8209","DOI":"10.1073\/pnas.0708308105","article-title":"Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin","volume":"105","author":"Parsonage","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1074\/jbc.RA120.014010_bib12","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1126\/science.1063143","article-title":"Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion","volume":"294","author":"Ritz","year":"2001","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.014010_bib13","doi-asserted-by":"crossref","first-page":"6735","DOI":"10.1073\/pnas.0801986105","article-title":"Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways","volume":"105","author":"Faulkner","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1074\/jbc.RA120.014010_bib14","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.molcel.2007.11.029","article-title":"Mutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activity","volume":"29","author":"Yamamoto","year":"2008","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA120.014010_bib15","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.freeradbiomed.2013.07.036","article-title":"The thioredoxin antioxidant system","volume":"66","author":"Lu","year":"2014","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/jbc.RA120.014010_bib16","doi-asserted-by":"crossref","first-page":"10535","DOI":"10.1016\/S0021-9258(18)86980-0","article-title":"Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases","volume":"265","author":"Tartaglia","year":"1990","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.014010_bib17","doi-asserted-by":"crossref","first-page":"6579","DOI":"10.1128\/jb.178.22.6579-6586.1996","article-title":"Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes","volume":"178","author":"Bsat","year":"1996","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA120.014010_bib18","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1038\/nrmicro3032","article-title":"The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium","volume":"11","author":"Imlay","year":"2013","journal-title":"Nat. Rev. Microbiol"},{"key":"10.1074\/jbc.RA120.014010_bib19","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.jsb.2015.11.004","article-title":"Low resolution solution structure of an enzymatic active AhpC10:AhpF2 ensemble of the Escherichia coli alkyl hydroperoxide reductase","volume":"193","author":"Kamariah","year":"2016","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.RA120.014010_bib20","doi-asserted-by":"crossref","first-page":"269","DOI":"10.2323\/jgam.47.269","article-title":"Molecular cloning and transcriptional analysis of the alkyl hydroperoxide reductase genes from Pseudomonas putida KT2442","volume":"47","author":"Fukumori","year":"2001","journal-title":"J. Gen. Appl. Microbiol"},{"key":"10.1074\/jbc.RA120.014010_bib21","doi-asserted-by":"crossref","first-page":"1380","DOI":"10.4014\/jmb.1503.03031","article-title":"Molecular analysis of promoter and intergenic region attenuator of the Vibrio vulnificus prx1ahpF operon","volume":"25","author":"Lee","year":"2015","journal-title":"J. Microbiol. Biotechnol"},{"key":"10.1074\/jbc.RA120.014010_bib22","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1038\/nrmicro1947","article-title":"Towards environmental systems biology of Shewanella","volume":"6","author":"Fredrickson","year":"2008","journal-title":"Nat. Rev. Microbiol"},{"key":"10.1074\/jbc.RA120.014010_bib23","doi-asserted-by":"crossref","first-page":"1752","DOI":"10.1038\/ismej.2013.62","article-title":"Combined effect of loss of the caa3 oxidase and Crp regulation drives Shewanella to thrive in redox-stratified environments","volume":"7","author":"Zhou","year":"2013","journal-title":"ISME J"},{"key":"10.1074\/jbc.RA120.014010_bib24","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1128\/JB.01077-13","article-title":"Protection from oxidative stress relies mainly on derepression of OxyR-dependent katBdps in Shewanella oneidensis","volume":"196","author":"Jiang","year":"2014","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA120.014010_bib25","doi-asserted-by":"crossref","first-page":"2179","DOI":"10.1128\/JB.00154-15","article-title":"Unraveling the mechanism for the viability deficiency of Shewanella oneidensis oxyR null mutant","volume":"197","author":"Shi","year":"2015","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA120.014010_bib26","doi-asserted-by":"crossref","first-page":"1821","DOI":"10.1111\/1462-2920.12418","article-title":"Managing oxidative stresses in Shewanella oneidensis: intertwined roles of the OxyR and OhrR regulons","volume":"16","author":"Li","year":"2014","journal-title":"Environ. Microbiol"},{"key":"10.1074\/jbc.RA120.014010_bib27","doi-asserted-by":"crossref","first-page":"439","DOI":"10.3389\/fmicb.2019.00439","article-title":"Oxidized OxyR up-regulates ahpCF expression to suppress plating defects of oxyR- and catalase-deficient strains","volume":"10","author":"Wan","year":"2019","journal-title":"Front. Microbiol"},{"key":"10.1074\/jbc.RA120.014010_bib28","doi-asserted-by":"crossref","first-page":"e01700","DOI":"10.1128\/AEM.01700-19","article-title":"Distinct roles of Shewanella oneidensis thioredoxin in regulation of cellular responses to hydrogen and organic peroxides","volume":"85","author":"Feng","year":"2019","journal-title":"Appl. Environ. Microbiol"},{"key":"10.1074\/jbc.RA120.014010_bib29","doi-asserted-by":"crossref","first-page":"e01919","DOI":"10.1128\/AEM.01989-19","article-title":"Complex oxidation of apocytochromes c during bacterial cytochrome c maturation","volume":"85","author":"Guo","year":"2019","journal-title":"Appl. Environ. Microbiol"},{"key":"10.1074\/jbc.RA120.014010_bib30","doi-asserted-by":"crossref","first-page":"4085","DOI":"10.1074\/jbc.RA117.001530","article-title":"Defining the binding determinants of Shewanella oneidensis OxyR: implications for the link between the contracted OxyR regulon and adaptation","volume":"293","author":"Wan","year":"2018","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.014010_bib31","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1016\/j.bbalip.2018.06.020","article-title":"Roles of multiple KASIII homologues of Shewanella oneidensis in initiation of fatty acid synthesis and in cerulenin resistance","volume":"1863","author":"Meng","year":"2018","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA120.014010_bib32","doi-asserted-by":"crossref","first-page":"D129","DOI":"10.1093\/nar\/gkq971","article-title":"WebGeSTer DB\u2014a transcription terminator database","volume":"39","author":"Mitra","year":"2011","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.RA120.014010_bib33","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/j.tibs.2015.05.001","article-title":"Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling","volume":"40","author":"Perkins","year":"2015","journal-title":"Trends Biochem. Sci"},{"key":"10.1074\/jbc.RA120.014010_bib34","doi-asserted-by":"crossref","first-page":"5159","DOI":"10.1038\/s41598-017-05354-5","article-title":"AhpC of the mycobacterial antioxidant defense system and its interaction with its reducing partner Thioredoxin-C","volume":"7","author":"Wong","year":"2017","journal-title":"Sci. Rep"},{"key":"10.1074\/jbc.RA120.014010_bib35","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1089\/ars.2016.6922","article-title":"Experimentally dissecting the origins of peroxiredoxin catalysis","volume":"28","author":"Nelson","year":"2018","journal-title":"Antioxid. Redox Signal"},{"key":"10.1074\/jbc.RA120.014010_bib36","doi-asserted-by":"crossref","first-page":"e75610","DOI":"10.1371\/journal.pone.0075610","article-title":"Unique organizational and functional features of the cytochrome c maturation system in Shewanella oneidensis","volume":"8","author":"Jin","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.RA120.014010_bib37","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1111\/mmi.12865","article-title":"Shewanella oneidensis cytochrome c maturation component CcmI is essential for heme attachment at the non-canonical motif of nitrite reductase NrfA","volume":"95","author":"Fu","year":"2015","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA120.014010_bib38","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1128\/MMBR.00001-09","article-title":"Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control","volume":"73","author":"Kranz","year":"2009","journal-title":"Microbiol. Mol. Biol. Rev"},{"key":"10.1074\/jbc.RA120.014010_bib39","doi-asserted-by":"crossref","first-page":"1190","DOI":"10.1126\/science.289.5482.1190","article-title":"Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase","volume":"289","author":"Lennon","year":"2000","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.014010_bib40","doi-asserted-by":"crossref","first-page":"9203","DOI":"10.1074\/jbc.M209888200","article-title":"Catalytic mechanism of thiol peroxidase from Escherichia coli: sulfenic acid formation and overoxidation of essential CYS61","volume":"278","author":"Baker","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.014010_bib41","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1021\/bi501515w","article-title":"Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC","volume":"54","author":"Parsonage","year":"2015","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.014010_bib42","doi-asserted-by":"crossref","first-page":"4620","DOI":"10.1111\/febs.13522","article-title":"NMR studies reveal a novel grab and release mechanism for efficient catalysis of the bacterial 2-Cys peroxiredoxin machinery","volume":"282","author":"Nartey","year":"2015","journal-title":"FEBS J"},{"key":"10.1074\/jbc.RA120.014010_bib43","doi-asserted-by":"crossref","first-page":"2848","DOI":"10.1107\/S1399004714019233","article-title":"Structure, mechanism and ensemble formation of the alkylhydroperoxide reductase subunits AhpC and AhpF from Escherichia coli","volume":"70","author":"Dip","year":"2014","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA120.014010_bib44","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1021\/bi951887s","article-title":"Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins","volume":"35","author":"Poole","year":"1996","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.014010_bib45","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/j.abb.2003.11.021","article-title":"Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis","volume":"423","author":"Jaeger","year":"2004","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.RA120.014010_bib46","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1126\/science.1067798","article-title":"Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein","volume":"295","author":"Bryk","year":"2002","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.014010_bib47","doi-asserted-by":"crossref","first-page":"6667","DOI":"10.1074\/jbc.M117.775858","article-title":"Essential role of the flexible linker on the conformational equilibrium of bacterial peroxiredoxin reductase for effective regeneration of peroxiredoxin","volume":"292","author":"Kamariah","year":"2017","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.014010_bib48","doi-asserted-by":"crossref","first-page":"5228","DOI":"10.1074\/jbc.M113.510248","article-title":"Mycothiol\/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis","volume":"289","author":"Hugo","year":"2014","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.014010_bib49","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/j.freeradbiomed.2011.04.023","article-title":"Oxidizing substrate specificity of Mycobacterium tuberculosis alkyl hydroperoxide reductase E: kinetics and mechanisms of oxidation and overoxidation","volume":"51","author":"Reyes","year":"2011","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/jbc.RA120.014010_bib50","doi-asserted-by":"crossref","first-page":"12330","DOI":"10.1016\/S0021-9258(18)63862-1","article-title":"The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid","volume":"264","author":"Poole","year":"1989","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.014010_bib51","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/S0079-6603(04)78003-4","article-title":"Flavoprotein disulfide reductases: advances in chemistry and function","volume":"78","author":"Argyrou","year":"2004","journal-title":"Prog. Nucleic Acid Res. Mol. Biol"},{"key":"10.1074\/jbc.RA120.014010_bib52","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.abb.2015.08.012","article-title":"Microbial oxidative stress response: novel insights from environmental facultative anaerobic bacteria","volume":"584","author":"Fu","year":"2015","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.RA120.014010_bib53","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1126\/science.1103185","article-title":"Accumulation of Mn(II) in Deinococcus radiodurans facilitates \u03b3-radiation resistance","volume":"306","author":"Daly","year":"2004","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.014010_bib54","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1021\/acssynbio.8b00485","article-title":"Regulatory NADH\/NAD+ redox biosensor for bacteria","volume":"8","author":"Liu","year":"2019","journal-title":"ACS Synth. Biol"},{"key":"10.1074\/jbc.RA120.014010_bib55","doi-asserted-by":"crossref","first-page":"3181","DOI":"10.1111\/1462-2920.12457","article-title":"Evidence for function overlapping of CymA and the cytochrome bc1 complex in the Shewanella oneidensis nitrate and nitrite respiration","volume":"16","author":"Fu","year":"2014","journal-title":"Environ. Microbiol"},{"key":"10.1074\/jbc.RA120.014010_bib56","doi-asserted-by":"crossref","first-page":"2198","DOI":"10.1111\/1462-2920.12091","article-title":"Crp-dependent cytochrome bd oxidase confers nitrite resistance to Shewanella oneidensis","volume":"15","author":"Fu","year":"2013","journal-title":"Environ. Microbiol"},{"key":"10.1074\/jbc.RA120.014010_bib57","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1002\/mbo3.224","article-title":"Regulation of nitrite resistance of the cytochrome cbb3 oxidase by cytochrome c ScyA in Shewanella oneidensis","volume":"4","author":"Yin","year":"2015","journal-title":"MicrobiologyOpen"},{"key":"10.1074\/jbc.RA120.014010_bib58","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/S0076-6879(94)33021-2","article-title":"Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides","volume":"233","author":"Wolff","year":"1994","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.RA120.014010_bib59","doi-asserted-by":"crossref","first-page":"e1594","DOI":"10.21769\/BioProtoc.1594","article-title":"Pyridine hemochromagen assay for determining the concentration of heme in purified protein solutions","volume":"5","author":"Barr","year":"2015","journal-title":"Bio Protoc"},{"key":"10.1074\/jbc.RA120.014010_bib60","doi-asserted-by":"crossref","first-page":"e51643","DOI":"10.1371\/journal.pone.0051643","article-title":"A Crp-dependent two-component system regulates nitrate and nitrite respiration in Shewanella oneidensis","volume":"7","author":"Dong","year":"2012","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.RA120.014010_bib61","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1038\/nprot.2009.2","article-title":"Protein structure prediction on the Web: a case study using the Phyre server","volume":"4","author":"Kelley","year":"2009","journal-title":"Nat. Protoc"},{"key":"10.1074\/jbc.RA120.014010_bib62","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1126\/science.1080405","article-title":"Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling","volume":"300","author":"Wood","year":"2003","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.014010_bib63","doi-asserted-by":"crossref","first-page":"37610","DOI":"10.1038\/srep37610","article-title":"Transition steps in peroxide reduction and a molecular switch for peroxide robustness of prokaryotic peroxiredoxins","volume":"6","author":"Kamariah","year":"2016","journal-title":"Sci. Rep"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925817492076?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925817492076?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA120.014010","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,18]],"date-time":"2021-12-18T05:53:08Z","timestamp":1639806788000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925817492076"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,8]]},"references-count":63,"journal-issue":{"issue":"32","published-print":{"date-parts":[[2020,8]]}},"alternative-id":["S0021925817492076"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra120.014010","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2020,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Plasticity of the peroxidase AhpC links multiple substrates to diverse disulfide-reducing pathways in Shewanella oneidensis","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA120.014010","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Feng et al.","name":"copyright","label":"Copyright"}]}}