2e81: Difference between revisions
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<StructureSection load='2e81' size='340' side='right'caption='[[2e81]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2e81' size='340' side='right'caption='[[2e81]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2e81]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2e81]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_succinogenes Vibrio succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E81 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HOA:HYDROXYAMINE'>HOA</scene>, <scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HOA:HYDROXYAMINE'>HOA</scene>, <scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fs7|1fs7]], [[1fs8|1fs8]], [[1fs9|1fs9]], [[2e80|2e80]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fs7|1fs7]], [[1fs8|1fs8]], [[1fs9|1fs9]], [[2e80|2e80]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nitrite_reductase_(cytochrome;_ammonia-forming) Nitrite reductase (cytochrome; ammonia-forming)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.2 1.7.2.2] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e81 OCA], [https://pdbe.org/2e81 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e81 RCSB], [https://www.ebi.ac.uk/pdbsum/2e81 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e81 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/NRFA_WOLSU NRFA_WOLSU]] Plays a role in nitrite reduction.<ref>PMID:10672190</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Nitrite reductase|Nitrite reductase]] | *[[Cytochrome c nitrite reductase|Cytochrome c nitrite reductase]] | ||
*[[Nitrite reductase 3D structures|Nitrite reductase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:50, 5 May 2021
Cytochrome c Nitrite Reductase from Wolinella succinogenes with bound intermediate hydroxylamineCytochrome c Nitrite Reductase from Wolinella succinogenes with bound intermediate hydroxylamine
Structural highlights
Function[NRFA_WOLSU] Plays a role in nitrite reduction.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCytochrome c nitrite reductase catalyzes the six-electron reduction of nitrite to ammonia without the release of potential reaction intermediates, such as NO or hydroxylamine. On the basis of the crystallographic observation of reaction intermediates and of density functional calculations, we present a working hypothesis for the reaction mechanism of this multiheme enzyme which carries a novel lysine-coordinated heme group (Fe-Lys). It is proposed that nitrite reduction starts with a heterolytic cleavage of the N-O bond which is facilitated by a pronounced back-bonding interaction of nitrite coordinated through nitrogen to the reduced (Fe(II)) but not the oxidized (Fe(III)) active site iron. This step leads to the formation of an [FeNO](6) species and a water molecule and is further facilitated by a hydrogen bonding network that induces an electronic asymmetry in the nitrite molecule that weakens one N-O bond and strengthens the other. Subsequently, two rapid one-electron reductions lead to an [FeNO](8) form and, by protonation, to an Fe(II)-HNO adduct. Hereafter, hydroxylamine will be formed by a consecutive two-electron two-proton step which is dehydrated in the final two-electron reduction step to give ammonia and an additional water molecule. A single electron reduction of the active site closes the catalytic cycle. Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase.,Einsle O, Messerschmidt A, Huber R, Kroneck PM, Neese F J Am Chem Soc. 2002 Oct 2;124(39):11737-45. PMID:12296741[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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