9l6d: Difference between revisions

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'''Unreleased structure'''


The entry 9l6d is ON HOLD  until Paper Publication
==the crystal structure of Azurin-LBT==
<StructureSection load='9l6d' size='340' side='right'caption='[[9l6d]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9l6d]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9L6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9L6D FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9l6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9l6d OCA], [https://pdbe.org/9l6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9l6d RCSB], [https://www.ebi.ac.uk/pdbsum/9l6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9l6d ProSAT]</span></td></tr>
</table>
== Function ==
[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 ==
Photoredox catalysis in protein systems presents exciting opportunities to achieve sustainable and efficient enzymatic reactions driven by light. Here, we report the design and characterization of PhotoNiR, an engineered azurin-based protein incorporating a red copper center and a lanthanide-binding tag (LBT). This dual-metal system enables photoredox reduction of nitrite to nitric oxide via a proposed donor-f-electron-acceptor (D-f-A) electron transfer mechanism. Upon photoirradiation, aromatic residues in the LBT donate electrons to the lanthanide ion, which relays them to the Cu(II) center, reducing it to Cu(I). The reduced Cu(I)-PhotoNiR catalyzes the reduction of NO(2) (-), and the generated NO subsequently reacts with free cysteine residues to form S-nitrosothiol (SNO) species. Spectroscopic and structural characterization confirmed that the copper center retains the properties of a red copper site and that the lanthanide-binding tag supports efficient electron transfer. This work represents one of the first examples of a D-f-A mechanism in a protein system, demonstrating the potential of integrating metalloprotein engineering with lanthanide photochemistry to develop novel photoenzymes for light-driven catalysis.


Authors:  
Engineering a Hetero-Bimetallic Azurin Photoenzyme for Photoredox Nitrite Reduction and SNO Adduct Formation.,Su B, Yu Y, Liu H, Li C Chemistry. 2025 Apr 15;31(22):e202500143. doi: 10.1002/chem.202500143. Epub 2025 , Mar 15. PMID:40038049<ref>PMID:40038049</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9l6d" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Liu H]]
[[Category: Su B]]
[[Category: Yu Y]]
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