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https://doi.org/10.5562/cca3047

Xanthine Dehydrogenase Active Site: Chiral Switching and Substrate Coordination

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

Puni tekst: engleski, pdf (2 MB) str. 439-447 preuzimanja: 1.683* citiraj
APA 6th Edition
Ilich, P. (2016). Xanthine Dehydrogenase Active Site: Chiral Switching and Substrate Coordination. Croatica Chemica Acta, 89 (4), 439-447. https://doi.org/10.5562/cca3047
MLA 8th Edition
Ilich, Predrag-Peter. "Xanthine Dehydrogenase Active Site: Chiral Switching and Substrate Coordination." Croatica Chemica Acta, vol. 89, br. 4, 2016, str. 439-447. https://doi.org/10.5562/cca3047. Citirano 24.09.2021.
Chicago 17th Edition
Ilich, Predrag-Peter. "Xanthine Dehydrogenase Active Site: Chiral Switching and Substrate Coordination." Croatica Chemica Acta 89, br. 4 (2016): 439-447. https://doi.org/10.5562/cca3047
Harvard
Ilich, P. (2016). 'Xanthine Dehydrogenase Active Site: Chiral Switching and Substrate Coordination', Croatica Chemica Acta, 89(4), str. 439-447. https://doi.org/10.5562/cca3047
Vancouver
Ilich P. Xanthine Dehydrogenase Active Site: Chiral Switching and Substrate Coordination. Croatica Chemica Acta [Internet]. 2016 [pristupljeno 24.09.2021.];89(4):439-447. https://doi.org/10.5562/cca3047
IEEE
P. Ilich, "Xanthine Dehydrogenase Active Site: Chiral Switching and Substrate Coordination", Croatica Chemica Acta, vol.89, br. 4, str. 439-447, 2016. [Online]. https://doi.org/10.5562/cca3047

Sažetak
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, Mo(VI), to the (R)-absolute configuration, SPY-5-43-C, for the fully reduced metal center, Mo(IV). 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.

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

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

Hrčak ID: 179538

URI
https://hrcak.srce.hr/179538

Posjeta: 1.887 *