Redox properties of tyrosine and related molecules

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

Style

An error occurred while generating the citation.

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

Additional Information

© 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Received 10 October 2011. Revised 4 December 2011. Accepted 12 December 2011. Available online 26 December 2011. Edited by Miguel Teixeira and Ricardo O. Louro. Dedicated to the memory of Antonio Xavier, an outstanding scientist and dear friend. We thank Seiji Yamada, Julie Hoy and Jens Kaiser for assistance with X-ray structure determination. Our work is supported by NIH (DK019038 to H.B.G. and J.R.W.; GM095037 to J.J.W.). The Gordon and Betty Moore Foundation supports the Molecular Observatory at Caltech, and NIH and DOE support operation of the Stanford Synchrotron Radiation Laboratory (SSRL) beamline 12-2.

Attached Files

Accepted Version - nihms346445.pdf

Files

nihms346445.pdf

Files (1.5 MB)

Name	Size	Download all
nihms346445.pdf md5:57ecb1a19dea0e6a8ef2967e6be003d4	1.5 MB	Preview Download

Additional details

	All versions	This version
Views	0	0
Downloads	0	0
Data volume	0 Bytes	0 Bytes