| Article ID | Journal | Published Year | Pages | File Type | 
|---|---|---|---|---|
| 2050241 | FEBS Letters | 2008 | 5 Pages | 
Abstract
												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.
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											Authors
												Anna Lewin, Lars Hederstedt, 
											