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Heme binding properties of heterologously expressed spinach cytochrome b 6 : Implications for transmembrane b ‐type cytochrome formation
Author(s) -
Dreher Carolin,
Prodöhl Alexander,
Weber Mathias,
Schneider Dirk
Publication year - 2007
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/j.febslet.2007.05.007
Subject(s) - cytochrome , cytochrome b , cytochrome p450 reductase , cytochrome c , biochemistry , heme , coenzyme q – cytochrome c reductase , cytochrome b6f complex , transmembrane protein , chemistry , cytochrome c peroxidase , cytochrome c1 , hemeprotein , heterologous expression , biology , enzyme , receptor , recombinant dna , mitochondrion , mitochondrial dna , gene
In vivo and in vitro requirements for the formation of cytochrome b 6 were examined to analyze the mechanisms of transmembrane b ‐type cytochrome formation. After heterologous expression of spinach cytochrome b 6 , formation of the holo‐cytochrome was observed within the E. coli inner membrane. The transmembrane orientation of cytochrome b 6 appeared not to be critical for heme binding and holo‐cytochrome formation. Furthermore, in vitro reconstitution of cytochrome b 6 was possible under oxidizing as well as under reducing conditions. Taken together these observations strongly indicate that transmembrane b ‐type cytochromes can spontaneously assemble in vitro as well as in a membrane.