6G50

The structure of thiocyanate dehydrogenase from Thioalkalivibrio paradoxus as isolated.

Replaces:  5F30

Summary for 6G50

• Entry DOI: 10.2210/pdb6g50/pdb
• Descriptor: Uncharacterized protein, COPPER (II) ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase, thiocyanate dehydrogenase, copper centers
• Biological source: Thioalkalivibrio paradoxus ARh 1
• Total number of polymer chains: 4
• Total formula weight: 208691.51

Authors

Polyakov, K.M.,Tsallagov, S.I.,Tikhkonova, T.V.,Popov, V.O. (deposition date: 2018-03-28, release date: 2019-04-10, Last modification date: 2024-01-17)

Primary citation

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.
Trinuclear copper biocatalytic center forms an active site of thiocyanate dehydrogenase.
Proc.Natl.Acad.Sci.USA, 117:5280-5290, 2020

PubMed 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.

PubMed: 32094184
DOI: 10.1073/pnas.1922133117

Experimental method

X-RAY DIFFRACTION (1.65 Å)