{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,31]],"date-time":"2025-10-31T06:58:10Z","timestamp":1761893890431},"reference-count":58,"publisher":"Microbiology Society","issue":"12","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2003,12,1]]},"abstract":"<jats:p>The cytoplasmic membrane protein CcmC is, together with other Ccm proteins, a component for the maturation of <jats:italic>c<\/jats:italic>-type cytochromes in Gram-negative bacteria. A <jats:italic>Pseudomonas fluorescens<\/jats:italic> ATCC 17400 <jats:italic>ccmC<\/jats:italic> mutant is cytochrome <jats:italic>c<\/jats:italic>-deficient and shows considerably reduced production of the two siderophores pyoverdine and quinolobactin, paralleled by a general inability to utilize various iron sources, with the exception of haem. The <jats:italic>ccmC<\/jats:italic> mutant accumulates in a 5-aminolevulinic acid-dependent synthesis a reddish, fluorescent pigment identified as protoporphyrin IX. As a consequence a <jats:italic>visA<\/jats:italic> phenotype similar to that of a ferrochelatase-deficient <jats:italic>hemH<\/jats:italic> mutant characterized by drastically reduced growth upon light exposure was observed for the <jats:italic>ccmC<\/jats:italic> mutant. The defect of iron\u2013protoporphyrin formation was further demonstrated by the failure of <jats:italic>ccmC<\/jats:italic> cell-free proteinase K-treated extracts to stimulate the growth of a haem auxotrophic <jats:italic>hemH<\/jats:italic> indicator strain, compared to similarly prepared wild-type extracts. In addition, the <jats:italic>ccmC<\/jats:italic> mutant did not sustain <jats:italic>hemH<\/jats:italic> growth in cross-feeding experiments while the wild-type did. Significantly reduced resistance to oxidative stress mediated by haem-containing catalases was observed for the <jats:italic>ccmC<\/jats:italic> mutant. A double <jats:italic>hemH ccmC<\/jats:italic> mutant could not be obtained in the presence of external haem without the <jats:italic>hemH<\/jats:italic> gene <jats:italic>in trans<\/jats:italic>, indicating that the combination of the two mutations is lethal. It was concluded that CcmC, apart from its known function in cytochrome <jats:italic>c<\/jats:italic> biogenesis, plays a role in haem biosynthesis. A function in the regulatory co-ordination of iron acquisition via siderophores, iron insertion into porphyrin via ferrochelatase and iron\u2013protoporphyrin export for cytochrome <jats:italic>c<\/jats:italic> formation is predicted.<\/jats:p>","DOI":"10.1099\/mic.0.26566-0","type":"journal-article","created":{"date-parts":[[2003,12,8]],"date-time":"2003-12-08T21:38:53Z","timestamp":1070919533000},"page":"3543-3552","source":"Crossref","is-referenced-by-count":17,"title":["Co-ordination of iron acquisition, iron porphyrin chelation and iron\u2013protoporphyrin export via the cytochrome c biogenesis protein CcmC in Pseudomonas fluorescens"],"prefix":"10.1099","volume":"149","author":[{"given":"Christine","family":"Baysse","sequence":"first","affiliation":[{"name":"Laboratory of Microbial Interactions, Department of Molecular and Cellular Interactions, Flanders Interuniversity Institute for Biotechnology, Vrije Universiteit Brussel, Building E, Room 6.6, Pleinlaan 2, B-1050 Brussels, 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