Structure/function correlations among coupled binuclear copper proteins through spectroscopic and reactivity studies of NspF.

ABSTRACT: The terminal step of 4-hydroxy-3-nitrosobenzamide biosynthesis in Streptomyces murayamaensis is performed by NspF, a mono-oxygenase that converts o-aminophenols to the corresponding nitroso product (hydroxyanilinase activity). Previous biochemical characterization of the resting form of NspF suggested that this enzyme belonged to the coupled binuclear copper enzyme (CBC) family. Another member of this enzyme family, tyrosinase, is able to mono-oxygenate monophenols (monophenolase activity) but not o-aminophenols. To gain insight into the unique reactivity of NspF, we have generated and characterized the oxy form of its active site. The observation of spectral features identical to those of oxy-tyrosinase indicates that oxy-NspF contains a Cu(2)O(2) core where peroxide is coordinated in a μ

SUBMITTER: Ginsbach JW 

PROVIDER: S-EPMC3390868 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature