Open AccessCopper acquisition by the SenC protein regulates aerobic respiration in Pseudomonas aeruginosa PAO1
Author(s) -
Frangipani Emanuela,
Haas Dieter
Publication year - 2009
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2009.01726.x
Subject(s) - cytochrome c oxidase , pseudomonas aeruginosa , periplasmic space , cytochrome , copper , oxidase test , mutant , biochemistry , microbiology and biotechnology , biology , electron transport complex iv , copper protein , yeast , chemistry , bacteria , gene , enzyme , genetics , escherichia coli , organic chemistry
Aerobic respiration of Pseudomonas aeruginosa involves four terminal oxidases belonging to the heme–copper family (that is, three cytochrome c oxidases and one quinol oxidase) plus one copper‐independent, cyanide‐insensitive quinol oxidase (CIO). The PA0114 gene encoding an SCO1/SenC‐type protein, which is known to be important for copper delivery to cytochrome c in yeast, Rhodobacter spp. and Agrobacterium tumefaciens , was found to be important for copper acquisition and aerobic respiration in P. aeruginosa . A PA0114 ( senC ) mutant grew poorly in low‐copper media and had low cytochrome cbb 3 ‐type oxidase activity, but expressed CIO at increased levels, by comparison with the wild‐type PAO1. Addition of copper reversed these phenotypes, suggesting that periplasmic copper capture by the SenC protein helps P. aeruginosa to adapt to copper deprivation.