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Updated: Aug 11, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Molybdenum and tungsten enzymes: the xanthine oxidase family
Carlos D Brondino1, Maria João Romão, Isabel Moura
1Facultad de Bioquímica y Ciencias Biológicas, Universidad Nacional del Litoral, Campus Universitario, 3000 Santa Fe, Argentina. brondino@fbcb.uni.edu.ar
Abstract:
Mononuclear molybdenum and tungsten are found in the active site of a diverse group of enzymes that, in general, catalyze oxygen atom transfer reactions. Enzymes of the xanthine oxidase family are the best-characterized mononuclear Mo-containing enzymes. Several 3D structures of diverse members of this family are known. Recently, the structures of substrate-bound and arsenite-inhibited forms of two members of this family have also been reported. In addition, spectroscopic studies have been utilized to elucidate fine details that complement the structural information. Altogether, these studies have provided an important amount of information on the characteristics of the active site and the electron transfer pathways.
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