{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T11:51:39Z","timestamp":1790509899144,"version":"4.1.0"},"reference-count":61,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2016,5,2]],"date-time":"2016-05-02T00:00:00Z","timestamp":1462147200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["GM101012"],"award-info":[{"award-number":["GM101012"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2016,7]]},"abstract":"<jats:title>Summary<\/jats:title>\n                  <jats:p>\n                    When sulfur compounds are scarce or difficult to process,\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    adapts by inducing the high\u2010level expression of sulfur\u2010compound importers. If cystine then becomes available, the cystine is rapidly overimported and reduced, leading to a burgeoning pool of intracellular cysteine. Most of the excess cysteine is exported, but some is adventitiously degraded, with the consequent release of sulfide. Sulfide is a potent ligand of copper and heme moieties, raising the prospect that it interferes with enzymes. We observed that when cystine was provided and sulfide levels rose,\n                    <jats:italic>E. coli<\/jats:italic>\n                    became strictly dependent upon cytochrome\n                    <jats:italic>bd<\/jats:italic>\n                    oxidase for continued respiration. Inspection revealed that low\u2010micromolar levels of sulfide inhibited the proton\u2010pumping cytochrome\n                    <jats:italic>bo<\/jats:italic>\n                    oxidase that is regarded as the primary respiratory oxidase. In the absence of the back\u2010up cytochrome\n                    <jats:italic>bd<\/jats:italic>\n                    oxidase, growth failed. Exogenous sulfide elicited the same effect. The potency of sulfide was enhanced when oxygen concentrations were low. Natural oxic\u2010anoxic interfaces are often sulfidic, including the intestinal environment where\n                    <jats:italic>E. coli<\/jats:italic>\n                    dwells. We propose that the sulfide resistance of the cytochrome\n                    <jats:italic>bd<\/jats:italic>\n                    oxidase is a key trait that permits respiration in such habitats.\n                  <\/jats:p>","DOI":"10.1111\/mmi.13372","type":"journal-article","created":{"date-parts":[[2016,3,18]],"date-time":"2016-03-18T21:13:45Z","timestamp":1458335625000},"page":"62-77","source":"Crossref","is-referenced-by-count":95,"title":["The cytochrome\n                    <i>bd<\/i>\n                    oxidase of\n                    <i>Escherichia coli<\/i>\n                    prevents respiratory inhibition by endogenous and exogenous hydrogen sulfide"],"prefix":"10.1111","volume":"101","author":[{"given":"Sergey","family":"Korshunov","sequence":"first","affiliation":[{"name":"Department of Microbiology University of Illinois Urbana IL 61801 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Karin R. 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