3u25

Publication Abstract from PubMed

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 (1.18A resolution) shows that H20 is strongly hydrogen bonded to Y48 (2.7-2.8A 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.

Redox properties of tyrosine and related molecules.,Warren JJ, Winkler JR, Gray HB FEBS Lett. 2012 Mar 9;586(5):596-602. Epub 2011 Dec 26. PMID:22210190^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.