5k91
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k91 OCA], [http://pdbe.org/5k91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k91 RCSB], [http://www.ebi.ac.uk/pdbsum/5k91 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k91 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k91 OCA], [http://pdbe.org/5k91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k91 RCSB], [http://www.ebi.ac.uk/pdbsum/5k91 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k91 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The heme enzyme chlorite dismutase (Cld) catalyzes the degradation of chlorite to chloride and dioxygen. Although structure and steady-state kinetics of Clds have been elucidated, many questions remain (e.g., the mechanism of chlorite cleavage and the pH dependence of the reaction). Here, we present high-resolution X-ray crystal structures of a dimeric Cld at pH 6.5 and 8.5, its fluoride and isothiocyanate complexes and the neutron structure at pH 9.0 together with the pH dependence of the Fe(III)/Fe(II) couple, and the UV-vis and resonance Raman spectral features. We demonstrate that the distal Arg127 cannot act as proton acceptor and is fully ionized even at pH 9.0 ruling out its proposed role in dictating the pH dependence of chlorite degradation. Stopped-flow studies show that (i) Compound I and hypochlorite do not recombine and (ii) Compound II is the immediately formed redox intermediate that dominates during turnover. Homolytic cleavage of chlorite is proposed. | ||
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| + | Molecular Mechanism of Enzymatic Chlorite Detoxification: Insights from Structural and Kinetic Studies.,Schaffner I, Mlynek G, Flego N, Puhringer D, Libiseller-Egger J, Coates L, Hofbauer S, Bellei M, Furtmuller PG, Battistuzzi G, Smulevich G, Djinovic-Carugo K, Obinger C ACS Catal. 2017 Nov 3;7(11):7962-7976. doi: 10.1021/acscatal.7b01749. Epub 2017, Oct 13. PMID:29142780<ref>PMID:29142780</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5k91" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:55, 31 January 2018
Crystal structure of dimeric chlorite dismutase from Cyanothece sp. PCC7425 in complex with fluoride
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