Redox properties of tyrosine and related molecules

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• 作者：Jeffrey J. Warren ; Jay R. Winkler ; Harry B. Gray<sup> ; sup><sup>hbgray@caltech.edusup>
• 关键词：Electron transfer ; Tyrosine ; Tyrosyl radical
• 刊名：FEBS Letters
• 出版年：2012
• 出版时间：9 March, 2012
• 年：2012
• 卷：586
• 期：5
• 页码：596-602
• 全文大小：478 K

文摘

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