6sg2: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: '''Unreleased structure''' The entry 6sg2 is ON HOLD Authors: Description: Category: Unreleased Structures |
No edit summary |
||
| (5 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==FeFe Hydrogenase from Desulfovibrio desulfuricans in Hinact state== | |||
<StructureSection load='6sg2' size='340' side='right'caption='[[6sg2]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SG2 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]] 1.65Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LFH:dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS 2kappaS)-mu-(oxomethylidene)diiron(2+)+sulphide'>LFH</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=6sg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sg2 OCA], [https://pdbe.org/6sg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sg2 RCSB], [https://www.ebi.ac.uk/pdbsum/6sg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sg2 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
[FeFe] hydrogenases are the most active H 2 converting catalysts in nature but their extreme oxygen sensitivity limits their use in technological applications. The [FeFe] hydrogenases from sulfate reducing bacteria can be purified in an O 2 -stable state called H inact . To date, the structure and mechanism of formation of H inact remain unknown. Our 1.65 A crystal structure of this state reveals a sulfur ligand bound to the open coordination site. Furthermore, in-depth spectroscopic characterization by X-ray absorption spectroscopy (XAS), nuclear resonance vibrational spectroscopy (NRVS), resonance Raman (RR) spectroscopy and infrared (IR) spectroscopy, together with hybrid quantum mechanical and molecular mechanical (QM/MM) calculations, provide detailed chemical insight into the H inact state and its mechanism of formation. This may facilitate the design of O 2 -stable hydrogenases and molecular catalysts. | |||
Caught in the Hinact: Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O2-stable State of [FeFe] Hydrogenase.,Rodriguez-Macia P, Galle L, Bjornsson R, Lorent C, Zebger I, Yoda Y, Cramer S, DeBeer S, Span I, Birrell J Angew Chem Int Ed Engl. 2020 Jun 2. doi: 10.1002/anie.202005208. PMID:32488975<ref>PMID:32488975</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6sg2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Galle LM]] | |||
[[Category: Span I]] | |||
