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Promoted evolution of a shortened variant of heme A synthase in the membrane of Bacillus subtilis
Author(s) -
Lewin Anna,
Hederstedt Lars
Publication year - 2008
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.2008.03.015
Subject(s) - bacillus subtilis , heme , heme a , biochemistry , mutagenesis , enzyme , mutant , atp synthase , transmembrane protein , residue (chemistry) , site directed mutagenesis , transmembrane domain , chemistry , membrane protein , mutant protein , biology , membrane , bacteria , genetics , receptor , gene
Bacillus subtilis heme A synthase is a membrane protein with 8 transmembrane segments. By using a two‐step mutagenesis approach we have generated and selected a fully functional enzyme protein variant with a seven residue internal deletion. The biochemical properties of the shortened variant are similar to those of the normal enzyme. This could indicate that residue H209 in the mutant protein substitutes for the missing H216 as an axial ligand to the heme iron. Our results provide insight in routes of membrane protein evolution and the structure of heme A synthases.