Published March 9, 2012
| Version Accepted Version
Journal Article
Open
Redox properties of tyrosine and related molecules
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
Additional details
Identifiers
- PMCID
- PMC3298607
- Eprint ID
- 29977
- DOI
- 10.1016/j.febslet.2011.12.014
- Resolver ID
- CaltechAUTHORS:20120404-105819558
Funding
- NIH
- DK019038
- NIH
- GM095037
- Gordon and Betty Moore Foundation
- Department of Energy (DOE)
Dates
- Created
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2012-04-04Created from EPrint's datestamp field
- Updated
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2021-11-09Created from EPrint's last_modified field