Work

Redox properties of tyrosine and related molecules

Year: 2011

Type: review

Abstract: 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.

Source: FEBS Letters

DOI: 10.1016/j.febslet.2011.12.014

Authors: Jeffrey J. Warren, Jay R. Winkler, Harry B. Gray

Institution: California Institute of Technology

Language: English

Topic: Metal-Catalyzed Oxygenation Mechanisms

Subfield: Inorganic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: bronze