View source for 9gyl


==Ferredoxin Wild-type -Oxidised state==
<StructureSection load='9gyl' size='340' side='right'caption='[[9gyl]], [[Resolution|resolution]] 1.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9gyl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9GYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9GYL 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]] 1.19&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9gyl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9gyl OCA], [https://pdbe.org/9gyl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9gyl RCSB], [https://www.ebi.ac.uk/pdbsum/9gyl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9gyl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FER1_SPIOL FER1_SPIOL] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The noncanonical amino acid, para-cyanophenylalanine (CNF), when incorporated into metalloproteins, functions as an infrared spectroscopic probe for the redox state of iron-sulfur clusters, offering a strategy for determining electron occupancy in the electron transport chains of complex metalloenzymes. A redshift of approximately 1-2 cm(-1) in the nitrile (NC) stretching frequency is observed, following reduction of spinach ferredoxin modified to contain CNF close to its [2Fe-2S] center, and this shift is reversed on re-oxidation. We extend this to CNF positioned near to the proximal [4Fe-4S] cluster of the [FeFe] hydrogenase from Desulfovibrio desulfuricans. In combination with a distal [4Fe-4S] cluster and the [4Fe-4S] cluster of the active site 'H-cluster' ([4Fe-4S](H)), the proximal cluster forms an electron relay connecting the active site to the surface of the protein. Again, a reversible shift in wavenumber for CNF is observed, following cluster reduction in either apo-protein (containing the iron-sulfur clusters but lacking the active site) or holo-protein with intact active site, demonstrating the general applicability of this approach to studying complex metalloenzymes.

Cyanophenylalanine as an Infrared Probe for Iron-Sulfur Cluster Redox State in Multicenter Metalloenzymes.,Duan Z, Wei J, Carr SB, Ramirez M, Evans RM, Ash PA, Rodriguez-Macia P, Sachdeva A, Vincent KA Chembiochem. 2025 May 10:e2500251. doi: 10.1002/cbic.202500251. PMID:40347495<ref>PMID:40347495</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9gyl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Spinacia oleracea]]
[[Category: Carr SB]]
[[Category: Vincent KA]]
[[Category: Wei J]]