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Despite its remarkable adaptability, little is known about the mechanisms of stress resistance in this bacterium. Here, in a screen for iron-susceptible transposon mutants, we identified a cytochrome\n              <jats:italic>bd<\/jats:italic>\n              that protects\n              <jats:italic>C. violaceum<\/jats:italic>\n              against multiple stresses. The two subunits of this cytochrome\n              <jats:italic>bd<\/jats:italic>\n              (CioAB) are encoded by the\n              <jats:italic>cioRAB<\/jats:italic>\n              operon, which also encodes a GbsR-type MarR family transcription factor (CioR). A \u2206\n              <jats:italic>cioAB<\/jats:italic>\n              mutant strain was sensitive to iron and the iron-requiring antibiotic streptonigrin and showed a decrease in siderophore production. Growth curves and survival assays revealed that the \u2206\n              <jats:italic>cioAB<\/jats:italic>\n              strain was also sensitive to zinc, hydrogen peroxide, nitric oxide, sulfide, and cyanide. Expression analysis showed that the promoter activity of the\n              <jats:italic>cioRAB<\/jats:italic>\n              operon and the transcript levels of the\n              <jats:italic>cioAB<\/jats:italic>\n              genes were increased in a \u2206\n              <jats:italic>cioR<\/jats:italic>\n              mutant. CioR bound the promoter region of the\n              <jats:italic>cio<\/jats:italic>\n              operon\n              <jats:italic>in vitro<\/jats:italic>\n              , indicating that CioR is a direct repressor of its own operon. Expression of the\n              <jats:italic>cio<\/jats:italic>\n              operon increased at high cell density and was dependent on the quorum-sensing regulator CviR. As cyanide is also a signal for\n              <jats:italic>cio<\/jats:italic>\n              expression, and production of endogenous cyanide is known to be a quorum sensing-regulated trait in\n              <jats:italic>C. violaceum<\/jats:italic>\n              , we suggest that CioAB is a cyanide-insensitive terminal oxidase that allows respiration under cyanogenic growth conditions. Our findings indicate that the cytochrome\n              <jats:italic>bd<\/jats:italic>\n              CioAB protects\n              <jats:italic>C. violaceum<\/jats:italic>\n              against multiple stress agents that are potentially produced endogenously or during interactions with a host.\n            <\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>IMPORTANCE<\/jats:title>\n            <jats:p>\n              The terminal oxidases of bacterial respiratory chains rely on heme-copper (heme-copper oxidases) or heme (cytochrome\n              <jats:italic>bd<\/jats:italic>\n              ) to catalyze the reduction of molecular oxygen to water.\n              <jats:italic>Chromobacterium violaceum<\/jats:italic>\n              is a facultative anaerobic bacterium that uses oxygen and other electron acceptors for respiration under conditions of varying oxygen availability. The\n              <jats:italic>C. violaceum<\/jats:italic>\n              genome encodes multiple respiratory terminal oxidases, but their role and regulation remain unexplored. Here, we demonstrate that CioAB, the single cytochrome\n              <jats:italic>bd<\/jats:italic>\n              from\n              <jats:italic>C. violaceum<\/jats:italic>\n              , protects this bacterium against multiple stressors that are inhibitors of heme-copper oxidases, including nitric oxide, sulfide, and cyanide. CioAB also confers\n              <jats:italic>C. violaceum<\/jats:italic>\n              resistance to iron, zinc, and hydrogen peroxide. This cytochrome\n              <jats:italic>bd<\/jats:italic>\n              is encoded by the\n              <jats:italic>cioRAB<\/jats:italic>\n              operon, which is under direct repression by the MarR-type regulator CioR. In addition, the\n              <jats:italic>cioRAB<\/jats:italic>\n              operon responds to quorum sensing and to cyanide, suggesting a protective mechanism of increasing CioAB in the setting of high endogenous cyanide production.\n            <\/jats:p>\n          <\/jats:sec>","DOI":"10.1128\/aem.02360-24","type":"journal-article","created":{"date-parts":[[2025,1,24]],"date-time":"2025-01-24T14:00:23Z","timestamp":1737727223000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":6,"title":["A cytochrome\n            <i>bd<\/i>\n            repressed by a MarR family regulator confers resistance to metals, nitric oxide, sulfide, and cyanide in\n            <i>Chromobacterium violaceum<\/i>"],"prefix":"10.1128","volume":"91","author":[{"given":"Bianca B.","family":"Batista","sequence":"first","affiliation":[{"name":"Departamento de Biologia Celular e Molecular e Bioagentes Patog\u00eanicos, Faculdade de Medicina de Ribeir\u00e3o Preto, Universidade de S\u00e3o Paulo","place":["Ribeir\u00e3o Preto, Brazil"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vinicius M.","family":"de Lima","sequence":"additional","affiliation":[{"name":"Departamento de Biologia Celular e Molecular e Bioagentes Patog\u00eanicos, Faculdade de Medicina de Ribeir\u00e3o Preto, Universidade de S\u00e3o Paulo","place":["Ribeir\u00e3o Preto, Brazil"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"W. 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