Enzymes
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Reaction participants Show >> << Hide
- Name help_outline thiocyanate Identifier CHEBI:18022 (Beilstein: 1901207; CAS: 302-04-5) help_outline Charge -1 Formula CNS InChIKeyhelp_outline ZMZDMBWJUHKJPS-UHFFFAOYSA-M SMILEShelp_outline [S-]C#N 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
Fe(III)-[cytochrome c]
Identifier
RHEA-COMP:14399
Reactive part
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- Name help_outline Fe3+ Identifier CHEBI:29034 (CAS: 20074-52-6) help_outline Charge 3 Formula Fe InChIKeyhelp_outline VTLYFUHAOXGGBS-UHFFFAOYSA-N SMILEShelp_outline [Fe+3] 2D coordinates Mol file for the small molecule Search links Involved in 253 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline cyanate Identifier CHEBI:29195 (CAS: 71000-82-3,661-20-1) help_outline Charge -1 Formula CNO InChIKeyhelp_outline XLJMAIOERFSOGZ-UHFFFAOYSA-M SMILEShelp_outline [O-]C#N 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline sulfur Identifier CHEBI:26833 (CAS: 7704-34-9) help_outline Charge 0 Formula S InChIKeyhelp_outline NINIDFKCEFEMDL-UHFFFAOYSA-N SMILEShelp_outline [S] 2D coordinates Mol file for the small molecule Search links Involved in 16 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
Fe(II)-[cytochrome c]
Identifier
RHEA-COMP:10350
Reactive part
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- Name help_outline Fe2+ Identifier CHEBI:29033 (CAS: 15438-31-0) help_outline Charge 2 Formula Fe InChIKeyhelp_outline CWYNVVGOOAEACU-UHFFFAOYSA-N SMILEShelp_outline [Fe++] 2D coordinates Mol file for the small molecule Search links Involved in 266 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:63880 | RHEA:63881 | RHEA:63882 | RHEA:63883 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Trinuclear copper biocatalytic center forms an active site of thiocyanate dehydrogenase.
Tikhonova T.V., Sorokin D.Y., Hagen W.R., Khrenova M.G., Muyzer G., Rakitina T.V., Shabalin I.G., Trofimov A.A., Tsallagov S.I., Popov V.O.
Biocatalytic copper centers are generally involved in the activation and reduction of dioxygen, with only few exceptions known. Here we report the discovery and characterization of a previously undescribed copper center that forms the active site of a copper-containing enzyme thiocyanate dehydroge ... >> More
Biocatalytic copper centers are generally involved in the activation and reduction of dioxygen, with only few exceptions known. Here we report the discovery and characterization of a previously undescribed copper center that forms the active site of a copper-containing enzyme thiocyanate dehydrogenase (suggested EC 1.8.2.7) that was purified from the haloalkaliphilic sulfur-oxidizing bacterium of the genus <i>Thioalkalivibrio</i> ubiquitous in saline alkaline soda lakes. The copper cluster is formed by three copper ions located at the corners of a near-isosceles triangle and facilitates a direct thiocyanate conversion into cyanate, elemental sulfur, and two reducing equivalents without involvement of molecular oxygen. A molecular mechanism of catalysis is suggested based on high-resolution three-dimensional structures, electron paramagnetic resonance (EPR) spectroscopy, quantum mechanics/molecular mechanics (QM/MM) simulations, kinetic studies, and the results of site-directed mutagenesis. << Less
Proc Natl Acad Sci U S A 117:5280-5290(2020) [PubMed] [EuropePMC]