Reduction Potential Tuning of the Blue Copper Center in Pseudomonas aeruginosa Azurin by the Axial Methionine as Probed by Unnatural Amino Acids

The conserved axial ligand methionine 121 from Pseudomonas aeruginosa azurin (Az) has been replaced by isostructural unnatural amino acid analogues, oxomethionine (OxM), difluoromethionine (DFM), trifluoromethionine (TFM), selenomethionine (SeM), and norleucine (Nle) using expressed protein ligation...

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Veröffentlicht in:	Journal of the American Chemical Society 2006-12, Vol.128 (49), p.15608-15617
Hauptverfasser:	Garner, Dewain K, Vaughan, Mark D, Hwang, Hee Jung, Savelieff, Masha G, Berry, Steven M, Honek, John F, Lu, Yi
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acids - chemistry Amino Acids - metabolism Azurin - chemistry Azurin - metabolism Chemistry Copper - chemistry Exact sciences and technology General and physical chemistry Hydrogen Bonding Ligands Methionine - analogs & derivatives Methionine - chemistry Methionine - metabolism Models, Molecular Norleucine - chemistry Norleucine - metabolism Oxidation-Reduction Protein Conformation Pseudomonas aeruginosa - chemistry Selenomethionine - chemistry Selenomethionine - metabolism Spectrum Analysis
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Zusammenfassung:	The conserved axial ligand methionine 121 from Pseudomonas aeruginosa azurin (Az) has been replaced by isostructural unnatural amino acid analogues, oxomethionine (OxM), difluoromethionine (DFM), trifluoromethionine (TFM), selenomethionine (SeM), and norleucine (Nle) using expressed protein ligation. The replacements resulted in
ISSN:	0002-7863 1520-5126
DOI:	10.1021/ja062732i