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 (1.18Å 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Warren JJ,Winkler JR,Gray HB

doi

10.1016/j.febslet.2011.12.014

subject

Has Abstract

pub_date

2012-03-09 00:00:00

pages

596-602

issue

5

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(11)00886-6

journal_volume

586

pub_type

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