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Croatica Chemica Acta, Vol.89 No.4 December 2016. -

Analysis of electronic, structural and mechanistic parameters of the enzyme-substrate reaction of xanthine oxidase, a member of the xanthine dehydrogenase class of mono-molybdopterin oxidoreductive enzymes, shows that the molybdenum center in the enzyme active site acts as a reversible chiral switch. The metal center cycles from the S-absolute configuration, SPY-5-42-A, in the fully oxidized state, MoVI, to the R-absolute configuration, SPY-5-43-C, for the fully reduced metal center, MoIV. This process is complemented by induction of chirality at the substrate carbon center pro-SC → SC and is involved in the control of coordination and, likely, protonation of imino-centers of conjugated heterocyclic substrates in the enzyme active site.

This work is licensed under a Creative Commons Attribution 4.0 International License.

xanthine dehydrogenase; molybdopterin cofactor; oxidoreductive catalysis; first-principles electronic structure calculation; Mo-center chirality switching; enzyme-substrate coordination control

Autor: Predrag-Peter Ilich - ; Department of Biological Sciences, St. John’s University, New York City, NY 11439, USA

Fuente: http://hrcak.srce.hr/


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