3obp

Publication Abstract from PubMed

Urate oxidase (EC 1.7.3.3 or UOX) catalyzes the conversion of uric acid using gaseous molecular oxygen to 5-hydroxyisourate and hydrogen peroxide in absence of any cofactor or transition metal. The catalytic mechanism was investigated using X-ray diffraction, electron spin resonance spectroscopy (ESR), and quantum mechanics calculations. The X-ray structure of the anaerobic enzyme-substrate complex gives credit to substrate activation before the dioxygen fixation in the peroxo hole, where incoming and outgoing reagents (dioxygen, water, and hydrogen peroxide molecules) are handled. ESR spectroscopy establishes the initial monoelectron activation of the substrate without the participation of dioxygen. In addition, both X-ray structure and quantum mechanic calculations promote a conserved base oxidative system as the main structural features in UOX that protonates/deprotonates and activate the substrate into the doublet state now able to satisfy the Wigner's spin selection rule for reaction with molecular oxygen in its triplet ground state. Proteins 2011; (c) 2011 Wiley-Liss, Inc.

X-ray, ESR, and quantum mechanics studies unravel a spin well in the cofactor-less urate oxidase.,Gabison L, Chopard C, Colloc'h N, Peyrot F, Castro B, Hajji ME, Altarsha M, Monard G, Chiadmi M, Prange T Proteins. 2011 Jun;79(6):1964-76. doi: 10.1002/prot.23022. Epub 2011 Apr, 12. PMID:21491497^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.