3u25
From Proteopedia
(Difference between revisions)
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase. | [https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 (1.18A resolution) shows that H20 is strongly hydrogen bonded to Y48 (2.7-2.8A 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. | ||
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| + | Redox properties of tyrosine and related molecules.,Warren JJ, Winkler JR, Gray HB FEBS Lett. 2012 Mar 9;586(5):596-602. Epub 2011 Dec 26. PMID:22210190<ref>PMID:22210190</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3u25" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Azurin 3D structures|Azurin 3D structures]] | *[[Azurin 3D structures|Azurin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of P. aeruginoas azurin containing a Tyr-His hydrogen bonded pair
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