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 Lettjournal_title
FEBS lettersauthors
Warren JJ,Winkler JR,Gray HBdoi
10.1016/j.febslet.2011.12.014subject
Has Abstractpub_date
2012-03-09 00:00:00pages
596-602issue
5eissn
0014-5793issn
1873-3468pii
S0014-5793(11)00886-6journal_volume
586pub_type
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