The purification of the hydroxylase component of a 3 component methane monooxygenase from the type II methanotroph Methylosinus trichosporium OB3b is reported. The enzyme (240 kDa) has an (αβγ)2 subunit structure as observed for hydroxylases isolated from other Type I and Type II methanotrophs, but it exhibits a 5 to 10 fold higher specific activity and is isolated in 2 to 10 fold higher yield. EPR and Mössbauer spectra of the hydroxylase show that it contains a coupled iron center containing an even number of iron atoms. The spectra are similar to those of proteins known to contain oxo-bridged binuclear iron centers. The presence of such a center is unprecedented in a monooxygenase and suggests that a novel mechanism is utilized.
|Original language||English (US)|
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jul 15 1988|