Structure/function studies of arsenite oxidoreductase and xanthine oxidase
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چکیده
The recently solved X-ray crystal structure of the molybdenum-containing arsenite ox idoreductase from Alcaligenes fa ecalis, is discussed, keeping in view the known mechanistic and spectroscopic information regarding the protein in a structural context. In addi tion, recent mechan istic studies of );,janthine oxidase are covered , with the conclusion that the reaction meclianism is initiated by nuclcophilic attack of a Mo-OH group on substrate.
منابع مشابه
Turkey liver xanthine dehydrogenase: further observations on the reaction with arsenite.
The catalytically essential persulphide groups at the molybdenum centres of xanthine oxidase and xanthine dehydrogenase are essential to interaction with arsenite (Edmonson et al., 1972; Cleere et al., 1974) Inhibition of xanthine hydroxylation may result from arsenite forming a complex with the persulphides and vicinal thiol groups (Massey & Edmonson, 1970). The NADH-dichlorophenol-indophenol ...
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تاریخ انتشار 2012