Open AccessThe multicopper oxidase CutO confers copper tolerance to Rhodobacter capsulatus
Author(s) -
Wiethaus Jessica,
Wildner Günter F.,
Masepohl Bernd
Publication year - 2006
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.1574-6968.2005.00094.x
Subject(s) - multicopper oxidase , rhodobacter , operon , escherichia coli , biochemistry , oxidase test , chemistry , gene , bacteria , biology , enzyme , genetics , laccase , mutant
The cutO gene of the photosynthetic purple bacterium Rhodobacter capsulatus codes for a multicopper oxidase as demonstrated by the ability of the recombinant Strep‐tagged protein to oxidize several mono‐ and diphenolic compounds known as substrates of Escherichia coli CueO and multicopper oxidases from other organisms. The R. capsulatus cutO gene was shown to form part of a tri‐cistronic operon, orf635 – cutO – cutR . Expression of the cutO operon was repressed under low copper conditions by the product of the cutR gene. CutO conferred copper tolerance not only under aerobic conditions, as described for the well‐characterized E. coli multicopper oxidase CueO, but also under anaerobic conditions.