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A system for the heterologous expression of complex redox proteins in Rhodobacter capsulatus : characterisation of recombinant sulphite:cytochrome c oxidoreductase from Starkeya novella
Author(s) -
Kappler Ulrike,
McEwan Alastair G.
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03344-6
Subject(s) - rhodobacter , biochemistry , cofactor , heterologous expression , recombinant dna , biology , heterologous , oxidoreductase , protein subunit , cytochrome , heme , redox , hemeprotein , chemistry , enzyme , gene , mutant , organic chemistry
The phototrophic purple non‐sulfur bacterium Rhodobacter capsulatus expresses a wide variety of complex redox proteins in response to changing environmental conditions. Here we report the construction and evaluation of an expression system for recombinant proteins in that organism which makes use of the dor promoter from the same organism. A generic expression vector, pDorEX, was constructed and used to express sulphite:cytochrome c oxidoreductase from Starkeya novella , a heterodimeric protein containing both molybdenum and haem c . The recombinant protein was secreted to the periplasm and its biochemical properties were very similar to those of the native enzyme. The pDorEX system therefore seems to be potentially useful for heterologous expression of multi‐subunit proteins containing complex redox cofactors.