Replacement of the methionine axial ligand in cytochrome c550 by a lysine: effects on the haem electronic structure |
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Authors: | Ricardo O Louro Ellen C de Waal Marcellus Ubbink David L Turner |
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Affiliation: | Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal. |
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Abstract: | The prosthetic group of low-spin haem proteins is an iron porphyrin with two axial ligands, typically histidine, methionine or lysine. Determining the geometry of the axial ligands is an important step in structural characterisation, particularly in the paramagnetic oxidised forms. This work extends earlier studies of the hyperfine nuclear magnetic resonance (NMR) shifts of haem substituents in bis-His and His–Met cytochromes to His–Lys co-ordination in the M100K mutant of Paracoccus versutus cytochrome c550. The electronic structure of the His–Lys haem is shown to be similar to that produced by His–cyanide co-ordination, such that NMR can be used to determine the geometry of the His ligand. |
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Keywords: | Paramagnetic nuclear magnetic resonance Cytochrome c Solution structure Site-specific mutagenesis Axial ligand |
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