Accepted_test

Details of the structure and function of the bacterial thiocyanate dehydrogenase with the unique copper active site
by Varfolomeeva L.A. | Shipkov N.S. | Dergousova N.I. | Boyko K.M. | Tikhonova T.V. | Popov V.O. | Federal Research Centre «Fundamentals of Biotechnology», RAS | Federal Research Centre «Fundamentals of Biotechnology», RAS | Federal Research Centre «Fundamentals of Biotechnology», RAS | Federal Research Centre «Fundamentals of Biotechnology», RAS | Federal Research Centre «Fundamentals of Biotechnology», RAS | Federal Research Centre «Fundamentals of Biotechnology», RAS
Abstract ID: 590
Event: BGRS-abstracts
Sections: [Sym 3] Section “Structural biology of proteins nucleic acids and membranes”

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In the present work, the structure of the unique trinuclear copper center of thiocyanate dehydrogenase (TcDH) was investigated  by X-ray crystallography. The rearrangements of the TcDH active site during a catalytic reaction are characterized in detail based on near-atomic resolution structural data. The model of the substate binding is confirmed based on the structure of the enzyme complexes with inhibitors. Obtained data shed light on the mechanism of a catalytic reaction of TcDH.

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