Redox properties of tyrosine and related molecules

Redox reactions of tyrosine play key roles in many biological processes, including water oxidation and DNA synthesis. We first review the redox properties of tyrosine (and other phenols) in small molecules and related polypeptides, then report work on (H20)/(Y48)-modified Pseudomonas aeruginosa azur...

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Veröffentlicht in:	FEBS letters 2012-03, Vol.586 (5), p.596-602
Hauptverfasser:	Warren, Jeffrey J., Winkler, Jay R., Gray, Harry B.
Format:	Artikel
Sprache:	eng
Schlagworte:	Azurin - chemistry Azurin - metabolism BDFE bond dissociation free energy CHEM crystal structure Crystallography, X-Ray DEA diethanolamine DNA Electron transfer Histidine - chemistry Histidine - metabolism Hydrogen Bonding Models, Chemical Models, Molecular oxidation Oxidation-Reduction PCET phenols polypeptides Protein Conformation protein structure proton transfer proton-coupled electron transfer Pseudomonas aeruginosa Pseudomonas aeruginosa - metabolism Tris tris(hydroxymethyl)aminomethane tryptophan Tyrosine Tyrosine - chemistry Tyrosine - metabolism Tyrosyl radical YO YOH
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Zusammenfassung:	Redox reactions of tyrosine play key roles in many biological processes, including water oxidation and DNA synthesis. We first review the redox properties of tyrosine (and other phenols) in small molecules and related polypeptides, then report work on (H20)/(Y48)-modified Pseudomonas aeruginosa azurin. The crystal structure of this protein (1.18Å resolution) shows that H20 is strongly hydrogen bonded to Y48 (2.7–2.8Å tyrosine-O to histidine-N distance). A firm conclusion is that proper tuning of the tyrosine potential by a proton-accepting base is critical for biological redox functions.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/j.febslet.2011.12.014