AI Article Synopsis
- Researchers discovered a new copper center in a thiocyanate dehydrogenase enzyme from a sulfur-oxidizing bacterium found in saline alkaline soda lakes.
- This unique copper cluster consists of three copper ions arranged in a triangular shape and enables the conversion of thiocyanate into cyanate, elemental sulfur, and two reducing agents without using molecular oxygen.
- The study includes detailed structural and kinetic analyses, employing various techniques like EPR spectroscopy and QM/MM simulations, to propose a molecular mechanism for the enzyme's catalytic process.
Article Abstract
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 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.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7071890 | PMC |
| http://dx.doi.org/10.1073/pnas.1922133117 | DOI Listing |
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