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| Line 8: |
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7qze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qze OCA], [https://pdbe.org/7qze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qze RCSB], [https://www.ebi.ac.uk/pdbsum/7qze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qze ProSAT]</span></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=7qze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qze OCA], [https://pdbe.org/7qze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qze RCSB], [https://www.ebi.ac.uk/pdbsum/7qze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qze ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
| |
| [https://www.uniprot.org/uniprot/A0A7U8UU09_STRLI A0A7U8UU09_STRLI]
| |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| Controlling the reactivity of high-valent Fe(IV)-O catalytic intermediates, Compounds I and II, generated in heme enzymes upon reaction with dioxygen or hydrogen peroxide, is important for function. It has been hypothesized that the presence (wet) or absence (dry) of distal heme pocket water molecules can influence whether Compound I undergoes sequential one-electron additions or a concerted two-electron reduction. To test this hypothesis, we investigate the role of water in the heme distal pocket of a dye-decolorizing peroxidase utilizing a combination of serial femtosecond crystallography and rapid kinetic studies. In a dry distal heme site, Compound I reduction proceeds through a mechanism in which Compound II concentration is low. This reaction shows a strong deuterium isotope effect, indicating that reduction is coupled to proton uptake. The resulting protonated Compound II (Fe(IV)-OH) rapidly reduces to the ferric state, giving the appearance of a two-electron transfer process. In a wet site, reduction of Compound I is faster, has no deuterium effect, and yields highly populated Compound II, which is subsequently reduced to the ferric form. This work provides a definitive experimental test of the hypothesis advanced in the literature that relates sequential or concerted electron transfer to Compound I in wet or dry distal heme sites.
| |
|
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| Serial Femtosecond Crystallography Reveals the Role of Water in the One- or Two-Electron Redox Chemistry of Compound I in the Catalytic Cycle of the B-Type Dye-Decolorizing Peroxidase DtpB.,Lucic M, Wilson MT, Tosha T, Sugimoto H, Shilova A, Axford D, Owen RL, Hough MA, Worrall JAR ACS Catal. 2022 Nov 4;12(21):13349-13359. doi: 10.1021/acscatal.2c03754. Epub , 2022 Oct 18. PMID:36366763<ref>PMID:36366763</ref>
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|
| |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 7qze" style="background-color:#fffaf0;"></div>
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|
| |
|
| ==See Also== | | ==See Also== |
| *[[Plastocyanin 3D structures|Plastocyanin 3D structures]] | | *[[Plastocyanin 3D structures|Plastocyanin 3D structures]] |
| == References ==
| |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
