Structural highlights
Publication Abstract from PubMedBiocatalytic 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 Thioalkalivibrio 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. Trinuclear copper biocatalytic center forms an active site of thiocyanate dehydrogenase.,Tikhonova TV, Sorokin DY, Hagen WR, Khrenova MG, Muyzer G, Rakitina TV, Shabalin IG, Trofimov AA, Tsallagov SI, Popov VO Proc Natl Acad Sci U S A. 2020 Feb 24. pii: 1922133117. doi:, 10.1073/pnas.1922133117. PMID:32094184[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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