9gyn: Difference between revisions
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The | ==Ferredoxin Wild-type - Reduced state== | ||
<StructureSection load='9gyn' size='340' side='right'caption='[[9gyn]], [[Resolution|resolution]] 1.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9gyn]] 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=9GYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9GYN 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]] 1Å</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></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=9gyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9gyn OCA], [https://pdbe.org/9gyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9gyn RCSB], [https://www.ebi.ac.uk/pdbsum/9gyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9gyn 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9gyn" style="background-color:#fffaf0;"></div> | ||
[[Category: Carr | == References == | ||
[[Category: Wei | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Spinacia oleracea]] | |||
[[Category: Carr SB]] | |||
[[Category: Vincent KA]] | |||
[[Category: Wei J]] | |||
